L-aspartate, L-asparagine and L-alanine formation and turnover

Reversible aspartate and alanine transamination connects oxaloacetate and pyruvate to amino-acid metabolism in the sampled fungi, animals and plants. Glutamine-dependent asparagine synthetase amidates aspartate using ATP and glutamine amide nitrogen, releasing glutamate, AMP and diphosphate. Asparaginases instead hydrolyse asparagine to aspartate and ammonium without a glutamate cosubstrate. Cytosolic, mitochondrial and plant plastid aminotransferases provide different implementations; their net flux depends on substrates, compartment and physiological conditions. Plant plastids include both conventional AspAT and a distinct bifunctional aspartate/prephenate aminotransferase. Asparagine hydrolysis is optional at this formation/turnover boundary and uses structurally distinct asparaginase families in the demonstrated yeast and plant examples. Secreted yeast Asp3 is strain dependent. Alanine transamination is a parallel reaction, not an asserted chemical link in the aspartate/asparagine chain. The taxonomic envelope does not imply universal retention, identical compartments or simultaneous flux through every branch.

MODULE:aspartate_asparagine_metabolismDRAFTCONCRETEMetabolic Pathwaymodules/aspartate_asparagine_metabolism.yaml
L-aspartate biosynthetic processGO:0006532 L-asparagine biosynthetic processGO:0070981 L-asparagine catabolic processGO:0006530
YeastPathways:ASPBIO-PWY
aspartate biosynthesis (S. cerevisiae, SGD YeastPathways)
Source pathway: ASPAMINOTRANS-RXN (AAT1, AAT2) and PYRUVATE-CARBOXYLASE-RXN (PYC1, PYC2). The transamination is modelled; pyruvate carboxylation is oxaloacetate supply and is kept outside the module.
YeastPathways:ASPARTATESYN-PWY
L-aspartate biosynthesis (S. cerevisiae, SGD YeastPathways)
Aspartate aminotransferase reaction (AAT1, AAT2); assignments retained.
YeastPathways:ASPARAGINE-BIOSYNTHESIS-1
L-asparagine biosynthesis I (S. cerevisiae, SGD YeastPathways)
ASPAMINOTRANS-RXN (AAT1, AAT2) and ASNSYNB-RXN (ASN1, ASN2); assignments retained.
YeastPathways:ASPARAGINE-DEG2-PWY
asparagine degradation (S. cerevisiae, SGD YeastPathways)
ASPARAGHYD-RXN (ASP1, ASP3-1, ASP3-2, ASP3-3, ASP3-4) followed by ASPAMINOTRANS-RXN (AAT1, AAT2); assignments retained, with ASP1 and the ASP3 cluster separated by compartment.
YeastPathways:ALANINE-SYN2-PWY
L-alanine biosynthesis II (S. cerevisiae, SGD YeastPathways)
Alanine aminotransferase reaction (ALT1); assignment retained.
YeastPathways:ALANINE-DEG3-PWY
L-alanine degradation III (S. cerevisiae, SGD YeastPathways)
The same ALT1 reaction in the catabolic direction; assignment retained.
GO:0006532
L-aspartate biosynthetic process
Biological process of the aspartate transamination part.
GO:0070981
L-asparagine biosynthetic process
Biological process of the asparagine synthetase part.
GO:0006530
L-asparagine catabolic process
Biological process of the asparaginase part.
GO:0042852
L-alanine biosynthetic process
Biological process of the alanine transamination part (biosynthetic direction).
GO:0042853
L-alanine catabolic process
Biological process of the alanine transamination part (catabolic direction).
PMID:33397945
Autophagy sustains glutamate and aspartate synthesis in Saccharomyces cerevisiae during nitrogen starvation.
Isotope tracing identifies Aat2 as the major source of newly synthesized aspartate specifically during nitrogen starvation in the tested budding-yeast cultures.
suggesting that Aat2p is the major enzyme for aspartate synthesis under nitrogen starvation
PMID:9288922
Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted to the peroxisomes in oleate-grown Saccharomyces cerevisiae.
AAT2 encodes the cytosolic aspartate aminotransferase, which is also targeted to peroxisomes in oleate-grown cells.
We demonstrate that the gene AAT2 codes for the cytosolic and peroxisomal AAT activities.
PMID:9655342
Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase.
Yeast cytosolic AAT is a PLP-dependent homodimer with the fold and active-site residues of bacterial and animal aspartate aminotransferases.
PMID:1482685
AAT1, a gene encoding a mitochondrial aspartate aminotransferase in Saccharomyces cerevisiae.
Sequence analysis identified AAT1 as a likely mitochondrial AspAT; subsequent mitochondrial-enzyme work provides stronger compartment/function support.
which is likely to be the yeast mitochondrial AspAT
PMID:22010850
Inactivation of mitochondrial aspartate aminotransferase contributes to the respiratory deficit of yeast frataxin-deficient cells.
Mitochondrial Aat1 participates in the malate-aspartate NADH shuttle; aat1 deletion causes respiratory deficiency.
deletion of the AAT1 gene in a wild-type strain caused respiratory deficiency
PMID:35621265
Cytosolic aspartate aminotransferase moonlights as a ribosome-binding modulator of Gcn2 activity during oxidative stress.
Aat2 also binds ribosomes and restrains Gcn2 activation during oxidative stress, independently of catalysis; this regulatory role is outside the module.
PMID:8951815
Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding factor.
ASN1 and ASN2 encode redundant asparagine synthetases; only the double disruption is an asparagine auxotroph.
Simultaneous disruption of both genes leads to a total asparagine auxotrophy, while disruption of asn1 or asn2 alone has no effect on growth under tested conditions.
PMID:8026756
The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase.
S. cerevisiae has an intracellular asparaginase I (ASP1) and a cell-wall asparaginase II (ASP3), which are homologous.
Saccharomyces cerevisiae produces two L-asparaginases (ASPs), intracellular ASP I and cell-wall ASP II.
PMID:27824095
Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity.
Purified recombinant Asp1 hydrolyses L-asparagine.
ScASNase1 has specific activity of 196.2 U/mg
PMID:3042786
Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene.
ASP3 encodes asparaginase II, which is under nitrogen catabolite repression.
nitrogen catabolite repression of asparaginase II is achieved by alteration in mRNA levels
PMID:22776361
The ASP3 locus in Saccharomyces cerevisiae originated by horizontal gene transfer from Wickerhamomyces.
The 2012 phylogenetic study proposed recent horizontal transfer of ASP3. Its strain-restricted distribution remains relevant, but later genome sampling and synteny favor ancestral presence followed by losses; recent transfer is not treated as settled.
is completely absent from the genomes of 128 diverse fungal species
PMID:17308034
Effect of 21 different nitrogen sources on global gene expression in the yeast Saccharomyces cerevisiae.
Cited by YeastPathways for asparagine as a nitrogen source (ASPARAGINE-DEG2-PWY).
PMID:19396236
ALT1-encoded alanine aminotransferase plays a central role in the metabolism of alanine in Saccharomyces cerevisiae.
Alt1 is the sole route of alanine synthesis and catabolism under respiratory conditions; under fermentative conditions alanine is made mainly by an Alt1-independent route.
under respiratory conditions, Alt1p constitutes the sole pathway for alanine biosynthesis and catabolism
PMID:23049841
Paralogous ALT1 and ALT2 retention and diversification have generated catalytically active and inactive aminotransferases in Saccharomyces cerevisiae.
The ALT2 paralog encodes a catalytically inactive protein, so only ALT1 is a module participant.
only Alt1 displays alanine aminotransferase activity; in contrast ALT2 encodes a catalytically inert protein
PMID:35697072
Evolutionary origin and functional diversification of aminotransferases.
Comparative review supports PLP-dependent amino/keto-acid exchange and substantial substrate diversification. Family membership alone does not establish a physiological substrate or net reaction direction.
PMID:33624365
Structural and functional diversity of asparaginases: Overview and recommendations for a revised nomenclature.
Asparaginase structural classes cross organismal boundaries; historical bacterial-type and plant-type names cannot delimit the module taxon scope.
PMID:34258001
Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.
Structural review separates Class 1 asparaginases from Class 2 N-terminal-nucleophile hydrolases and discusses potassium-dependent and independent plant enzymes. These labels do not mean bacterial-only or plant-only distribution.
PMID:31998641
Asparagine Synthetase in Cancer: Beyond Acute Lymphoblastic Leukemia.
Human ASNS review explains coupling of glutamine hydrolysis to ATP-dependent aspartate amidation. Its physiological glutamine requirement is distinguished from free-ammonia activity of purified recombinant human enzyme.
PMID:24902885
Plastidic aspartate aminotransferases and the biosynthesis of essential amino acids in plants.
Plant plastids contain conventional AspAT and a distinct bifunctional aspartate/prephenate aminotransferase; a cytosol/mitochondrion-only model misses this implementation.
PMID:40940428
Mapping multi-substrate specificity of Arabidopsis aminotransferases.
The 2025 Arabidopsis survey measured many substrate combinations and incorporated them into a metabolic model. This supports caution about one-name/one-substrate assumptions; the abstract alone does not establish native flux or an activity for a particular exemplar.
PMID:36040324
The evolution and role of the periplasmic asparaginase Asp3 in yeast.
Expanded Saccharomyces sampling and synteny favor ancestral ASP3 with repeated loss over recent acquisition. Heterologous ASP3 improves growth on sole asparagine in the tested host, but not in apple juice.
most likely to be an ancestral gene
PMID:12068109
Molecular and physiological analysis of Arabidopsis mutants defective in cytosolic or chloroplastic aspartate aminotransferase.
Arabidopsis ASP2 defects reduce aspartate and asparagine pools in specific alleles/tissues. ASP5 mutants retain residual activity and do not establish absolute dispensability of plastid aspartate formation.
PMID:9535706
Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana.
Purified Arabidopsis ASP1/ASP2/ASP5 enzymes were kinetically characterized with the four AspAT substrates. This supports conventional plant AspAT chemistry; the older plastid subtype assignment was tentative.
PMID:2573597
The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity.
Mutating the human ASNS N-terminal cysteine abolishes glutamine-dependent activity while retaining ammonia-dependent synthesis in vitro, separating glutamine hydrolysis from the synthetase reaction.
PMID:2564390
Expression of human asparagine synthetase in Escherichia coli.
Purified recombinant human ASNS has both glutamine- and ammonia-dependent activity in vitro; this does not demonstrate a separate native ammonia-dependent pathway.
PMID:39502420
Mitochondrial aspartate aminotransferase ( maa1 ) inactivation causes glutamate-requiring glu1 mutation in Schizosaccharomyces pombe.
Fission-yeast maa1 inactivation produces a glutamate requirement; its prevailing biosynthetic direction is distinct from caa1-mediated aspartate formation in the tested conditions.
PMID:16705405
Co-occurrence of both L-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent L-asparaginase.
Purified Arabidopsis ASPGB1 exemplifies potassium-dependent plant Ntn asparaginase chemistry; its specificity must be read together with the later beta-aspartyl-peptide study.
PMID:22127737
Role of asparaginase variable loop at the carboxyl terminal of the alpha subunit in the determination of substrate preference in plants.
Direct Arabidopsis enzyme comparison establishes that potassium-dependent ASPGB1 can also hydrolyse beta-aspartyl-histidine; the asparaginase role does not mean absolute substrate exclusivity.
PMID:17319845
Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana.
Arabidopsis ALAAT1 contributes to alanine breakdown during recovery from hypoxia; this is physiological evidence for a conditional catabolic direction.
PMID:17451745
Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.
E. coli ansA (UniProtKB:P0A962) is a cytosolic Class 1 biochemical comparator for substrate-responsive asparaginase behavior; it does not extend the eukaryotic module taxon envelope.
PMID:2407723
Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins.
E. coli ansB (UniProtKB:P00805) is a periplasmic Class 1 comparator. Its Gram-negative outer-membrane-bounded periplasm differs from the fungal cell-wall-bounded compartment.
PMID:20883697
Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis.
Target comparison distinguishes bifunctional Arabidopsis PAT from conventional ASP5, which retains AspAT activity without detectable prephenate activity under the reported assay conditions.
PMID:28011691
CORRECTION.
Correction to PMID:25070637 reidentifies mutant labels/plasmids and revises mutant-specific activity claims; the remeasured wild-type bifunctional enzyme result remains supported.

Review literature, primary evidence, family placement and source-model assertions were checked separately. Detailed reference assessments and explicit uncertainties are recorded in the references and module notes; module boundaries do not redefine which broader GO processes a gene may participate in.

12Nodes
4Parts
2Variant Sets
7Variants
9Annotons
2Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:aspartate_asparagine_metabolism deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ every leaf node grounds to a representative protein.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Reaction chaining (advisory)

✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.

  • aspartate_transamination_step → asparagine_synthetase_step [NOT_CHECKED]
    The shared metabolite is L-aspartate, not a CoA carrier. Native plant Asp/Asn pool coupling and purified ASNS chemistry support the link; cross-compartment transfer is outside the catalytic boundary.
  • asparaginase_step → aspartate_transamination_step [NOT_CHECKED]
    L-aspartate is the hydrolysis product and the substrate of reverse transamination. The AspAT leaf displays its forward biosynthetic orientation; this edge explicitly uses the reverse direction. Transport is required for the periplasmic implementation.

Function consistency and core coverage

25 gene-function check(s) reflected in core functions · 0 conflict(s) · 2 evidence or coverage gap(s) (34 comparison(s))

Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.

AnnotonParticipantFunctionAssessment
cytosolic_aspartate_aminotransferase_activity AAT2 (Saccharomyces cerevisiae)
UniProtKB:P23542
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cytosolic_aspartate_aminotransferase_activity caa1 (Schizosaccharomyces pombe)
UniProtKB:O42652
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cytosolic_aspartate_aminotransferase_activity GOT1 (Homo sapiens)
UniProtKB:P17174
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cytosolic_aspartate_aminotransferase_activity ASP2 (Arabidopsis thaliana)
UniProtKB:P46645
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
mitochondrial_aspartate_aminotransferase_activity AAT1 (Saccharomyces cerevisiae)
UniProtKB:Q01802
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
mitochondrial_aspartate_aminotransferase_activity maa1 (Schizosaccharomyces pombe)
UniProtKB:O94320
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
mitochondrial_aspartate_aminotransferase_activity GOT2 (Homo sapiens)
UniProtKB:P00505
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
plastid_conventional_aspartate_aminotransferase_activity ASP5 (Arabidopsis thaliana)
UniProtKB:P46248
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
plastid_bifunctional_aspartate_aminotransferase_activity PAT (Arabidopsis thaliana)
UniProtKB:Q9SIE1
Family Representative 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
asparagine_synthetase_activity ASN1 (Saccharomyces cerevisiae)
UniProtKB:P49089
Family Representative 		asparagine synthase (glutamine-hydrolyzing) activity
GO:0004066 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
asparagine_synthetase_activity ASN2 (Saccharomyces cerevisiae)
UniProtKB:P49090
Family Representative 		asparagine synthase (glutamine-hydrolyzing) activity
GO:0004066 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
asparagine_synthetase_activity asn1 (Schizosaccharomyces pombe)
UniProtKB:P78753
Family Representative 		asparagine synthase (glutamine-hydrolyzing) activity
GO:0004066 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
asparagine_synthetase_activity ASNS (Homo sapiens)
UniProtKB:P08243
Family Representative 		asparagine synthase (glutamine-hydrolyzing) activity
GO:0004066 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
asparagine_synthetase_activity ASN2 (Arabidopsis thaliana)
UniProtKB:Q9LV77
Family Representative 		asparagine synthase (glutamine-hydrolyzing) activity
GO:0004066 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
intracellular_asparaginase_activity ASP1 (Saccharomyces cerevisiae)
UniProtKB:P38986
Family Representative 		asparaginase activity
GO:0004067 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cell_wall_asparaginase_activity ASP3-1 (Saccharomyces cerevisiae)
UniProtKB:P0CZ17
Family Representative 		asparaginase activity
GO:0004067 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cell_wall_asparaginase_activity ASP3-2 (Saccharomyces cerevisiae)
UniProtKB:P0CX77
Family Representative 		asparaginase activity
GO:0004067 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cell_wall_asparaginase_activity ASP3-3 (Saccharomyces cerevisiae)
UniProtKB:P0CX78
Family Representative 		asparaginase activity
GO:0004067 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cell_wall_asparaginase_activity ASP3-4 (Saccharomyces cerevisiae)
UniProtKB:P0CX79
Family Representative 		asparaginase activity
GO:0004067 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
plant_ntn_asparaginase_activity ASPGB1 (Arabidopsis thaliana)
UniProtKB:Q8GXG1
Family Representative 		asparaginase activity
GO:0004067 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
alanine_aminotransferase_activity ALT1 (Saccharomyces cerevisiae)
UniProtKB:P52893
Family Representative 		L-alanine:2-oxoglutarate transaminase activity
GO:0004021 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
alanine_aminotransferase_activity alt1 (Schizosaccharomyces pombe)
UniProtKB:Q10334
Family Representative 		L-alanine:2-oxoglutarate transaminase activity
GO:0004021 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
alanine_aminotransferase_activity GPT (Homo sapiens)
UniProtKB:P24298
Family Representative 		L-alanine:2-oxoglutarate transaminase activity
GO:0004021 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
alanine_aminotransferase_activity GPT2 (Homo sapiens)
UniProtKB:Q8TD30
Family Representative 		L-alanine:2-oxoglutarate transaminase activity
GO:0004021 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
alanine_aminotransferase_activity ALAAT1 (Arabidopsis thaliana)
UniProtKB:F4I7I0
Family Representative 		L-alanine:2-oxoglutarate transaminase activity
GO:0004021 		Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cytosolic_aspartate_aminotransferase_activity aspartate aminotransferases (cytosolic isozymes)
PANTHER:PTHR11879
Family 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Family Supported
Family review supports GO:0004069 FAMILY_WIDE. Shared by the cytosolic and mitochondrial eukaryotic isozymes and by bacterial AspC. PAINT places it at the eukaryotic mitochondrial-type node, the cytosolic node and a gammaproteobacterial AspC node. TyrB also transaminates aspartate, but its physiological role is aromatic; the fungal secondary-metabolism members (tasG, ucdG) were not checked. The aspartate/asparagine and malate-aspartate shuttle modules use the family id with compartment-specific representatives, which is appropriate.
mitochondrial_aspartate_aminotransferase_activity aspartate aminotransferases (mitochondrial isozymes)
PANTHER:PTHR11879
Family 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Family Supported
Family review supports GO:0004069 FAMILY_WIDE. Shared by the cytosolic and mitochondrial eukaryotic isozymes and by bacterial AspC. PAINT places it at the eukaryotic mitochondrial-type node, the cytosolic node and a gammaproteobacterial AspC node. TyrB also transaminates aspartate, but its physiological role is aromatic; the fungal secondary-metabolism members (tasG, ucdG) were not checked. The aspartate/asparagine and malate-aspartate shuttle modules use the family id with compartment-specific representatives, which is appropriate.
plastid_conventional_aspartate_aminotransferase_activity Plastid conventional AspAT
PANTHER:PTHR11879:SF46
Family 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Family Supported
Family review supports GO:0004069 FAMILY_WIDE. Shared by the cytosolic and mitochondrial eukaryotic isozymes and by bacterial AspC. PAINT places it at the eukaryotic mitochondrial-type node, the cytosolic node and a gammaproteobacterial AspC node. TyrB also transaminates aspartate, but its physiological role is aromatic; the fungal secondary-metabolism members (tasG, ucdG) were not checked. The aspartate/asparagine and malate-aspartate shuttle modules use the family id with compartment-specific representatives, which is appropriate.
plastid_bifunctional_aspartate_aminotransferase_activity Plastid bifunctional AspAT / prephenate aminotransferase
PANTHER:PTHR46383:SF1
Family 		L-aspartate:2-oxoglutarate transaminase activity
GO:0004069 		Family Review Missing
No supported structured family review is available for PANTHER:PTHR46383:SF1.
asparagine_synthetase_activity glutamine-dependent asparagine synthetases
PANTHER:PTHR11772
Family 		asparagine synthase (glutamine-hydrolyzing) activity
GO:0004066 		Family Supported
Family review supports GO:0004066 FAMILY_WIDE. The module's core activity for this family and a PAINT IBD at PTN000206334, the family root for the asparagine synthetases. Direct evidence exists in yeast (two cytosolic asparagine synthetases; double disruption gives total asparagine auxotrophy) and for recombinant human ASNS. All four gene reviews in the family (ASN1, ASN2, ASNS; asn1 is a stub) accept the IBA. The SF2 beta-lactam synthetases are excepted.
intracellular_asparaginase_activity L-asparaginases (intracellular)
PANTHER:PTHR11707
Family 		asparaginase activity
GO:0004067 		Family Supported
Family review supports GO:0004067 FAMILY_WIDE. The module's activity for both asparaginase variants (intracellular and cell-wall). Asserted by PAINT at PTN000194668 (fungal plus type II clade; seeds the five S. cerevisiae genes and E. coli ansB) and PTN008524626 (type I clade; seeds E. coli ansA, M. tuberculosis ansA, Thermococcus TK1656 and rat). Supported directly for yeast ASP1 (recombinant enzyme) and ASP3 (asparaginase II). The archaeal GatD subunits are excepted: six of them inherit the term from PTN008524626.
cell_wall_asparaginase_activity L-asparaginases (secreted, cell-wall or periplasmic)
PANTHER:PTHR11707
Family 		asparaginase activity
GO:0004067 		Family Supported
Family review supports GO:0004067 FAMILY_WIDE. The module's activity for both asparaginase variants (intracellular and cell-wall). Asserted by PAINT at PTN000194668 (fungal plus type II clade; seeds the five S. cerevisiae genes and E. coli ansB) and PTN008524626 (type I clade; seeds E. coli ansA, M. tuberculosis ansA, Thermococcus TK1656 and rat). Supported directly for yeast ASP1 (recombinant enzyme) and ASP3 (asparaginase II). The archaeal GatD subunits are excepted: six of them inherit the term from PTN008524626.
plant_ntn_asparaginase_activity Plant Ntn asparaginases with demonstrated asparagine hydrolysis
PANTHER:PTHR10188:SF13
Family 		asparaginase activity
GO:0004067 		Family Review Missing
No supported structured family review is available for PANTHER:PTHR10188:SF13.
alanine_aminotransferase_activity alanine aminotransferases
PANTHER:PTHR11751
Family 		L-alanine:2-oxoglutarate transaminase activity
GO:0004021 		Family Supported
Family review supports GO:0004021 FAMILY_WIDE. The module's core activity for this family. Experimentally shown for S. cerevisiae Alt1 (sole alanine-synthesising and alanine-catabolising transaminase under respiration) and asserted by PAINT at PTN002272157 from Arabidopsis ALAAT1/ALAAT2/GGAT1 and kinetoplastid seeds. PTN002272157 does not reach the fungal (ALT1, ALT2, alt1) or human (GPT, GPT2) members in the current PAINT GAF, so the yeast enzymes have no IBA for this term; that is a coverage gap, not evidence against the function. Alt2 is the one documented exception.

Gene-review completeness (25/25 grounded genes reviewed)

17 complete review(s) · 10 with deep research · 0 missing review · 15 reviewed but lacking deep research

Gene Review Complete Deep research
AAT1 Q01802 ✓ ✓ ✓
AAT2 P23542 ✓ ✓ ✓
ALAAT1 F4I7I0 ✓ 18/21 ✗
ALT1 P52893 ✓ ✓ ✓
alt1 Q10334 ✓ ✓ ✗
ASN1 P49089 ✓ ✓ ✓
asn1 P78753 ✓ ✓ ✗
ASN2 P49090 ✓ ✓ ✓
ASN2 Q9LV77 ✓ 9/11 ✗
ASNS P08243 ✓ 21/24 ✗
ASP1 P38986 ✓ ✓ ✓
ASP2 P46645 ✓ 17/25 ✗
ASP3-1 P0CZ17 ✓ 15/17 ✓
ASP3-2 P0CX77 ✓ ✓ ✓
ASP3-3 P0CX78 ✓ ✓ ✓
ASP3-4 P0CX79 ✓ ✓ ✓
ASP5 P46248 ✓ 26/31 ✗
caa1 O42652 ✓ ✓ ✗
GOT1 P17174 ✓ ✓ ✗
GOT2 P00505 ✓ ✓ ✗
GPT P24298 ✓ ✓ ✗
GPT2 Q8TD30 ✓ ✓ ✗
maa1 O94320 ✓ ✓ ✗
PAT Q9SIE1 ✓ 20/21 ✗
Q8GXG1 Q8GXG1 ✓ 4/5 ✗

Details

Context
EukaryotaNCBITaxon:2759
L-aspartate, L-asparagine and L-alanine formation and turnoverMetabolic Pathwayaspartate_asparagine_metabolism
L-aspartate biosynthetic processGO:0006532 L-asparagine biosynthetic processGO:0070981 L-asparagine catabolic processGO:0006530
Context
EukaryotaNCBITaxon:2759

Boundary: aspartate/asparagine formation and turnover plus parallel alanine transamination. Oxaloacetate/pyruvate supply, membrane transport, ammonium assimilation, the complete malate-aspartate shuttle and downstream aromatic/aspartate-family amino-acid pathways remain adjacent processes. The core requires an AspAT implementation and glutamine-dependent ASNS; hydrolysis and alanine turnover are optional branches. No common compartment is imposed. Plant plastid PAT is included only for AspAT chemistry; ASP5 is not assigned PAT activity. E. coli ansA/ansB are independently reviewed biochemical comparators for Class 1 asparaginases, not eukaryotic participant exemplars: ansB occupies an outer-membrane-bounded periplasm, not the fungal cell-wall-bounded compartment. The three cached YeastPathways imports place AAT1 and, in the degradation model, ASP3 in cytosol; target evidence governs their compartments here. Pyruvate carboxylase is upstream substrate supply at this chosen boundary; its broader GO process annotation is not declared erroneous for that reason. PomBase maa1 and caa1 retain reversible AspAT chemistry, but their prevalent physiological directions differ in PMID:39502420. Alt1 matrix localization is a curated inference, not disproved by transit-peptide length alone. Aat2 ribosome/Gcn2 regulation and peroxisomal targeting on oleate remain documented gene-level context outside the cytosolic implementation. ASP3 evolution is qualified by the later synteny study, and four identical S288C copies are not four independent biochemical experiments.

Connections

Aspartate made by forward AspAT chemistry supplies glutamine-dependent ASNS. This is metabolite continuity, not direct physical channeling; compartment-specific transport can intervene.
PMID:12068109
Molecular and physiological analysis of Arabidopsis mutants defective in cytosolic or chloroplastic aspartate aminotransferase.
Native ASP2 alleles affect both Asp and Asn pools, supporting precursor coupling.
PMID:2573597
The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity.
Human ASNS directly carries out glutamine-dependent aspartate amidation.
PMID:8951815
Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding factor.
Yeast ASNS paralog loss establishes the downstream synthetic requirement.
gomodel:YeastPathways_ASPARAGINE-BIOSYNTHESIS-1
The live model contains four RO:0002413 edges from AAT1/AAT2 activities to ASN1/ASN2 activities. This independently corroborates the curated precursor relationship, without proving physical substrate channeling.
Asparaginase releases aspartate that can enter the reverse AspAT reaction to form oxaloacetate and glutamate. Extracellular Asp3 requires substrate import; the connection does not assert obligatory flux or a futile synthesis/hydrolysis cycle.
PMID:36040324
The evolution and role of the periplasmic asparaginase Asp3 in yeast.
The yeast assimilation scheme distinguishes extracellular hydrolysis, transport and intracellular Asp conversion to oxaloacetate/glutamate.
PMID:27824095
Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity.
Purified yeast Asp1 supports the hydrolytic first reaction.
PMID:9535706
Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana.
Four-substrate kinetics establish reversible plant AspAT chemistry.
Part 1: aspartate formation by transamination
Reversible oxaloacetate / L-aspartate transamination with glutamate / 2-oxoglutarateReactionaspartate_transamination_step
L-aspartate biosynthetic processGO:0006532

The displayed substrates/products orient the reaction toward aspartate formation. Catabolic turnover and mitochondrial glutamate supply use its reverse direction; no universal net flux is implied.

Variant set: Aspartate aminotransferase isozyme by compartment by compartment (One Or More)

Cytosolic and mitochondrial AspATs are demonstrated in the sampled opisthokonts; plants additionally use plastid isozymes from two families. Compartment and substrate use must be verified per member. Aat2 predominance is demonstrated under nitrogen starvation, not every yeast condition.

Cytosolic aspartate aminotransferaseReactioncytosolic_aspartate_aminotransferase

Annotons

Cytosolic aspartate aminotransferase
cytosolic_aspartate_aminotransferase_activity
Participant: Family: AAT2 / caa1 / GOT1 (cytosolic AspAT)
Gene:
AAT2 / caa1 / GOT1 (cytosolic AspAT)
Family:
aspartate aminotransferases (cytosolic isozymes)PANTHER:PTHR11879 Function-restricted cytosolic members of PTHR11879, with distinct fungal, human and Arabidopsis subfamilies. A family or subfamily name is not a compartment annotation.
Representative Members: AAT2 (Saccharomyces cerevisiae)UniProtKB:P23542 caa1 (Schizosaccharomyces pombe)UniProtKB:O42652 GOT1 (Homo sapiens)UniProtKB:P17174 ASP2 (Arabidopsis thaliana)UniProtKB:P46645
Required Function:
L-aspartate:2-oxoglutarate transaminase activityGO:0004069

Function

L-aspartate:2-oxoglutarate transaminase activityGO:0004069
Substrates: oxaloacetate L-glutamate
Products: L-aspartate 2-oxoglutarate

Locations

cytosolGO:0005829

Reversible cytosolic exchange. Aat2 supplies newly synthesized aspartate during nitrogen starvation; Arabidopsis ASP2 affects Asp/Asn pools. These conditions do not establish the same dominant flux in every species.

PMID:33397945
Autophagy sustains glutamate and aspartate synthesis in Saccharomyces cerevisiae during nitrogen starvation.
Target-specific isotope tracing supports starvation-associated aspartate formation.
PMID:12068109
Molecular and physiological analysis of Arabidopsis mutants defective in cytosolic or chloroplastic aspartate aminotransferase.
Native Arabidopsis ASP2 mutants connect cytosolic Asp formation with downstream Asn pools.
PMID:9535706
Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana.
Purified plant enzyme supports reversible four-substrate AspAT chemistry.
Mitochondrial aspartate aminotransferaseReactionmitochondrial_aspartate_aminotransferase

Annotons

Mitochondrial aspartate aminotransferase
mitochondrial_aspartate_aminotransferase_activity
Participant: Family: AAT1 / maa1 / GOT2 (mitochondrial AspAT)
Gene:
AAT1 / maa1 / GOT2 (mitochondrial AspAT)
Family:
aspartate aminotransferases (mitochondrial isozymes)PANTHER:PTHR11879 Family-level id used because the fungal mitochondrial enzymes are in PTHR11879:SF22 and human GOT2 in SF39 (UniProt PANTHER cross-references), so no single subfamily spans the representatives.
Representative Members: AAT1 (Saccharomyces cerevisiae)UniProtKB:Q01802 maa1 (Schizosaccharomyces pombe)UniProtKB:O94320 GOT2 (Homo sapiens)UniProtKB:P00505
Required Function:
L-aspartate:2-oxoglutarate transaminase activityGO:0004069

Function

L-aspartate:2-oxoglutarate transaminase activityGO:0004069

Locations

mitochondrial matrixGO:0005759

Reversible mitochondrial AspAT chemistry. Budding-yeast Aat1 supports respiration/shuttle metabolism; fission-yeast maa1 predominantly supplies glutamate under tested conditions. Mammalian GOT2 can supply aspartate, with net flux context dependent.

PMID:22010850
Inactivation of mitochondrial aspartate aminotransferase contributes to the respiratory deficit of yeast frataxin-deficient cells.
Aat1 deletion and mitochondrial enzyme inactivation link this enzyme to respiratory metabolism.
PMID:39502420
Mitochondrial aspartate aminotransferase ( maa1 ) inactivation causes glutamate-requiring glu1 mutation in Schizosaccharomyces pombe.
Fission-yeast maa1 physiology demonstrates why identical AspAT chemistry does not imply universal aspartate-forming flux.
Plastid conventional AspATReactionplastid_conventional_aspartate_aminotransferase
Context
ViridiplantaeNCBITaxon:33090

Annotons

Plastid conventional AspAT
plastid_conventional_aspartate_aminotransferase_activity
Participant: Family: Plastid conventional AspAT
Family:
Plastid conventional AspATPANTHER:PTHR11879:SF46
Representative Members: ASP5 (Arabidopsis thaliana)UniProtKB:P46248
Required Function:
L-aspartate:2-oxoglutarate transaminase activityGO:0004069

Function

L-aspartate:2-oxoglutarate transaminase activityGO:0004069
Substrates: oxaloacetate L-glutamate
Products: L-aspartate 2-oxoglutarate

Locations

plastidGO:0009536

Plastid AspAT activity. ASP5 does not acquire prephenate activity merely because the neighboring PAT implementation is bifunctional.

PMID:9535706
Recombinant expression, purification, and characterization of three isoenzymes of aspartate aminotransferase from Arabidopsis thaliana.
Purified target enzyme supports AspAT chemistry; physiological pathway allocation is assessed separately.
PMID:24902885
Plastidic aspartate aminotransferases and the biosynthesis of essential amino acids in plants.
Comparative review identifies this distinct plastid implementation.
PMID:20883697
Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis.
Target comparison distinguishes bifunctional Arabidopsis PAT from conventional ASP5, which retains AspAT activity without detectable prephenate activity under the reported assay conditions.
Plastid bifunctional AspAT / prephenate aminotransferaseReactionplastid_bifunctional_aspartate_aminotransferase
Context
ViridiplantaeNCBITaxon:33090

Annotons

Plastid bifunctional AspAT / prephenate aminotransferase
plastid_bifunctional_aspartate_aminotransferase_activity
Participant: Family: Plastid bifunctional AspAT / prephenate aminotransferase
Family:
Plastid bifunctional AspAT / prephenate aminotransferasePANTHER:PTHR46383:SF1 PAT is assigned to PTHR46383:SF1 by the current UniProt record, whereas release-19 PANTHER classification files place Q9SIE1 in PTHR43795:SF2. Both source placements are retained by the member index. The selected current UniProt family is constrained by demonstrated AspAT activity; no evolutionary node or manual override is inferred.
Representative Members: PAT (Arabidopsis thaliana)UniProtKB:Q9SIE1
Required Function:
L-aspartate:2-oxoglutarate transaminase activityGO:0004069

Function

L-aspartate:2-oxoglutarate transaminase activityGO:0004069
Substrates: oxaloacetate L-glutamate
Products: L-aspartate 2-oxoglutarate

Locations

plastidGO:0009536

Bifunctional class-Ib enzyme with AspAT activity; prephenate transamination belongs to aromatic-amino-acid metabolism outside this module.

PMID:25070637
Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway.
Purified target enzyme supports AspAT chemistry; physiological pathway allocation is assessed separately.
PMID:24902885
Plastidic aspartate aminotransferases and the biosynthesis of essential amino acids in plants.
Comparative review identifies this distinct plastid implementation.
PMID:20883697
Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis.
Target comparison distinguishes bifunctional Arabidopsis PAT from conventional ASP5, which retains AspAT activity without detectable prephenate activity under the reported assay conditions.
PMID:28011691
CORRECTION.
Correction to PMID:25070637 reidentifies mutant labels/plasmids and revises mutant-specific activity claims; the remeasured wild-type bifunctional enzyme result remains supported.
Part 2: asparagine synthesis
Aspartate + glutamine + ATP + water to asparagine + glutamate + AMP + diphosphateReactionasparagine_synthetase_step
L-asparagine biosynthetic processGO:0070981

This leaf covers glutamine-dependent ASNS. Unrelated bacterial AsnA is outside the eukaryotic boundary. Free ammonia can substitute in vitro for the human enzyme, without establishing a separate native pathway or converting glutamine amidation into glutamate transamination.

Annotons

Glutamine-dependent asparagine synthetase
asparagine_synthetase_activity
Participant: Family: ASN1 / ASN2 / asn1 / ASNS (asparagine synthetase)
Gene:
ASN1 / ASN2 / asn1 / ASNS (asparagine synthetase)
Family:
glutamine-dependent asparagine synthetasesPANTHER:PTHR11772
Representative Members: ASN1 (Saccharomyces cerevisiae)UniProtKB:P49089 ASN2 (Saccharomyces cerevisiae)UniProtKB:P49090 asn1 (Schizosaccharomyces pombe)UniProtKB:P78753 ASNS (Homo sapiens)UniProtKB:P08243 ASN2 (Arabidopsis thaliana)UniProtKB:Q9LV77
Required Function:
asparagine synthase (glutamine-hydrolyzing) activityGO:0004066

Function

asparagine synthase (glutamine-hydrolyzing) activityGO:0004066
Substrates: L-aspartate L-glutamine ATP H2O
Products: L-asparagine L-glutamate AMP diphosphate

Locations

cytosolGO:0005829

Coupled glutamine hydrolysis and ATP-dependent aspartate amidation. Yeast ASN1/ASN2 are redundant in the tested growth conditions; Arabidopsis ASN2 has condition-specific nitrogen-allocation functions.

PMID:8951815
Cloning of the ASN1 and ASN2 genes encoding asparagine synthetases in Saccharomyces cerevisiae: differential regulation by the CCAAT-box-binding factor.
Double loss of yeast ASN1/ASN2 abolishes asparagine prototrophy under tested conditions.
PMID:2573597
The N-terminal cysteine of human asparagine synthetase is essential for glutamine-dependent activity.
Human enzyme mutagenesis separates glutamine-donor hydrolysis from the ammonia-using synthetase component.
PMID:31998641
Asparagine Synthetase in Cancer: Beyond Acute Lymphoblastic Leukemia.
Review supports coupled human ASNS chemistry with the in-vitro ammonia caveat retained.
Part 3: asparagine hydrolysis (catabolic) (optional)
L-asparagine + H2O to L-aspartate + ammoniumReactionasparaginase_step
L-asparagine catabolic processGO:0006530
Variant set: Asparaginase by structural family and compartment by enzyme family / compartment / lineage (One Or More)

Yeast Class 1 Asp1/Asp3 and plant Class 2 Ntn enzymes provide alternative implementations. Historical bacterial-type and plant-type labels cross taxonomic boundaries. ASP3 is strain dependent; later comparative genomics challenges the older recent-transfer interpretation.

Intracellular asparaginaseReactionintracellular_asparaginase

Annotons

Intracellular asparaginase
intracellular_asparaginase_activity
Participant: Family: ASP1 (intracellular Class 1 asparaginase)
Gene:
ASP1 (intracellular Class 1 asparaginase)
Family:
L-asparaginases (intracellular)PANTHER:PTHR11707
Representative Members: ASP1 (Saccharomyces cerevisiae)UniProtKB:P38986
Required Function:
asparaginase activityGO:0004067

Function

asparaginase activityGO:0004067
Substrates: L-asparagine H2O
Products: L-aspartate ammonium

Locations

cytosolGO:0005829

Hydrolyses intracellular asparagine to aspartate and ammonium.

PMID:8026756
The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase.
Gene characterization establishes the intracellular yeast Asp1 isozyme.
PMID:27824095
Recombinant L-asparaginase 1 from Saccharomyces cerevisiae: an allosteric enzyme with antineoplastic activity.
Purified recombinant yeast Asp1 directly hydrolyses asparagine.
Cell-wall (extracellular) asparaginaseReactioncell_wall_asparaginase

Annotons

Cell-wall asparaginase
cell_wall_asparaginase_activity
Participant: Family: ASP3 (secreted Class 1 asparaginase)
Gene:
ASP3 (secreted Class 1 asparaginase)
Family:
L-asparaginases (secreted, cell-wall or periplasmic)PANTHER:PTHR11707 Selected secreted fungal members; cytoplasmic Asp1 belongs to the same family/subfamily. Family membership and ancestral presence of ASP3 do not imply periplasmic targeting of every homolog.
Representative Members: ASP3-1 (Saccharomyces cerevisiae)UniProtKB:P0CZ17 ASP3-2 (Saccharomyces cerevisiae)UniProtKB:P0CX77 ASP3-3 (Saccharomyces cerevisiae)UniProtKB:P0CX78 ASP3-4 (Saccharomyces cerevisiae)UniProtKB:P0CX79
Required Function:
asparaginase activityGO:0004067

Function

asparaginase activityGO:0004067

Locations

cell wall-bounded periplasmic spaceGO:0030287

Periplasmic hydrolysis of external asparagine in ASP3-positive yeast strains, regulated by nitrogen availability. Resulting aspartate/ammonium must cross the plasma membrane before intracellular use.

PMID:3042786
Asparaginase II of Saccharomyces cerevisiae. Characterization of the ASP3 gene.
ASP3 regulation and asparaginase-II characterization support extracellular asparagine use.
PMID:36040324
The evolution and role of the periplasmic asparaginase Asp3 in yeast.
Strain distribution, periplasmic hydrolysis and condition-specific growth effects support this optional yeast implementation.
Plant Ntn asparaginaseReactionplant_ntn_asparaginase
Context
ViridiplantaeNCBITaxon:33090

Annotons

Potassium-dependent plant Ntn asparaginase
plant_ntn_asparaginase_activity
Participant: Family: Plant Ntn asparaginases with demonstrated asparagine hydrolysis
Family:
Plant Ntn asparaginases with demonstrated asparagine hydrolysisPANTHER:PTHR10188:SF13
Representative Members: ASPGB1 (Arabidopsis thaliana)UniProtKB:Q8GXG1
Required Function:
asparaginase activityGO:0004067

Function

asparaginase activityGO:0004067
Substrates: L-asparagine H2O
Products: L-aspartate ammonium

Hydrolyses asparagine via a structurally distinct Ntn enzyme; the demonstrated potassium activation and peptide activity belong to this exemplar, not every member of the broad family.

PMID:16705405
Co-occurrence of both L-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent L-asparaginase.
Purified target enzyme establishes potassium-dependent asparagine hydrolysis.
PMID:22127737
Role of asparaginase variable loop at the carboxyl terminal of the alpha subunit in the determination of substrate preference in plants.
Later direct assays show that specificity is broader than an Asn-only description.
PMID:34258001
Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.
Structural review supports the distinction from yeast Class 1 enzymes.
Part 4: alanine formation and use by transamination (optional)
pyruvate + L-glutamate to L-alanine + 2-oxoglutarate (reversible)Reactionalanine_transamination_step
L-alanine biosynthetic processGO:0042852 L-alanine catabolic processGO:0042853

Annotons

Alanine aminotransferase
alanine_aminotransferase_activity
Participant: Family: ALT1 / alt1 / GPT / GPT2 (alanine aminotransferase)
Gene:
ALT1 / alt1 / GPT / GPT2 (alanine aminotransferase)
Family:
alanine aminotransferasesPANTHER:PTHR11751 S. cerevisiae ALT2 (P52892) is in the same subfamily but is catalytically inactive (PMID:23049841) and is not a representative.
Representative Members: ALT1 (Saccharomyces cerevisiae)UniProtKB:P52893 alt1 (Schizosaccharomyces pombe)UniProtKB:Q10334 GPT (Homo sapiens)UniProtKB:P24298 GPT2 (Homo sapiens)UniProtKB:Q8TD30 ALAAT1 (Arabidopsis thaliana)UniProtKB:F4I7I0
Required Function:
L-alanine:2-oxoglutarate transaminase activityGO:0004021

Function

L-alanine:2-oxoglutarate transaminase activityGO:0004021
Substrates: pyruvate L-glutamate
Products: L-alanine 2-oxoglutarate

Reversible alanine transamination. Respiratory budding yeast depends on Alt1 for both directions; fermenting cells have an additional biosynthetic route. Arabidopsis ALAAT1 contributes to post-hypoxic alanine catabolism. Mixed compartments are recorded per member, not imposed on the family.

PMID:19396236
ALT1-encoded alanine aminotransferase plays a central role in the metabolism of alanine in Saccharomyces cerevisiae.
Growth and flux context distinguish respiratory Alt1 dependence from fermentative alternative alanine formation.
PMID:23049841
Paralogous ALT1 and ALT2 retention and diversification have generated catalytically active and inactive aminotransferases in Saccharomyces cerevisiae.
Direct comparison shows why catalytically inactive Alt2 cannot be admitted by family membership alone.
PMID:17319845
Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana.
Native plant study supports condition-specific alanine breakdown.