id: Q9BYV1
gene_symbol: AGXT2
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  AGXT2 (alanine--glyoxylate aminotransferase 2) is a mitochondrial,
  pyridoxal-5'-phosphate (PLP)-dependent, class-III aminotransferase that
  functions as a homotetramer and has broad substrate specificity. It
  transaminates glyoxylate to glycine using L-alanine (or other amino acids) as
  the amino donor (alanine:glyoxylate transaminase, EC 2.6.1.44), contributing
  to glyoxylate detoxification, and it transaminates D-beta-aminoisobutyrate, a
  pyrimidine-catabolism end product (EC 2.6.1.40). AGXT2 is also the principal
  aminotransferase that metabolises the endogenous nitric-oxide-synthase
  inhibitors asymmetric and symmetric dimethylarginine (ADMA and SDMA), as well
  as N-monomethylarginine, converting them to (dimethylguanidino)valerate
  isomers; by lowering ADMA it can protect endothelial nitric oxide production.
  The mature enzyme is imported into the mitochondrion via a cleaved N-terminal
  transit peptide and resides in the mitochondrial matrix, with highest
  expression in kidney tubular epithelium and liver hepatocytes. AGXT2 activity
  is a modifier of plasma methylarginine and beta-aminoisobutyrate levels and of
  associated cardiovascular and renal phenotypes, and common coding variants
  (e.g. p.Val140Ile) reduce its activity.
alternative_products:
- name: '1'
  id: Q9BYV1-1
- name: '2'
  id: Q9BYV1-2
  sequence_note: VSP_055802
existing_annotations:
- term:
    id: GO:0042853
    label: L-alanine catabolic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Phylogenetically inferred involvement in L-alanine catabolism. AGXT2 uses
      L-alanine as the amino donor in its transaminase reactions (glyoxylate +
      L-alanine = glycine + pyruvate), consuming alanine, which is directly
      demonstrated experimentally for the human enzyme.
    action: ACCEPT
    reason: >-
      Consistent with the biochemistry: L-alanine is the physiological amino
      donor in the alanine:glyoxylate transaminase reaction, so alanine is
      catabolised. There is also a directly-supported IDA annotation to the same
      term (PMID:20018850).
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Catalyzes the conversion of glyoxylate to glycine using alanine as the"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: >-
      Phylogenetically inferred mitochondrial localization/activity. AGXT2
      carries a cleaved N-terminal mitochondrial transit peptide and its
      mitochondrial localization is directly demonstrated in human cells.
    action: ACCEPT
    reason: >-
      Strongly corroborated by direct experimental evidence (PMID:20018850,
      PMID:24586340, PMID:31818439) and by the UniProt-annotated transit
      peptide; the enzyme acts within the mitochondrion.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetically inferred alanine:glyoxylate transaminase activity
      (EC 2.6.1.44). This is the defining, namesake molecular function of AGXT2
      and is directly demonstrated for the human enzyme.
    action: ACCEPT
    reason: >-
      Core molecular function. Directly supported by IDA annotations
      (PMID:20018850, PMID:24586340) and by the UniProt catalytic-activity
      record; the IBA is at the correct level of specificity.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Reaction=glyoxylate + L-alanine = glycine + pyruvate"
- term:
    id: GO:0009436
    label: glyoxylate catabolic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Phylogenetically inferred role in glyoxylate catabolism. AGXT2
      transaminates glyoxylate to glycine, consuming (detoxifying) glyoxylate.
    action: ACCEPT
    reason: >-
      Consistent with the alanine:glyoxylate transaminase reaction; also
      supported by an IDA annotation to the same term (PMID:20018850). Note the
      dominant in vivo glyoxylate-to-glycine flux is peroxisomal (AGXT), but the
      AGXT2 reaction genuinely consumes glyoxylate.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Reaction=glyoxylate + L-alanine = glycine + pyruvate"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: >-
      Electronic annotation to mitochondrion (transferred from rat ortholog
      Q64565 and UniProt subcellular-location mapping). Consistent with the
      experimentally established mitochondrial localization of human AGXT2.
    action: ACCEPT
    reason: >-
      Correct localization, corroborated by multiple IDA/HTP annotations and the
      UniProt transit peptide.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: located_in
  review:
    summary: >-
      ARBA machine-learning electronic annotation to mitochondrial matrix. As a
      soluble matrix aminotransferase imported via a cleaved transit peptide,
      matrix localization is the expected and correct sub-compartment.
    action: ACCEPT
    reason: >-
      More specific than the mitochondrion annotation and biologically correct;
      Reactome also localizes the AGXT2 reaction to the mitochondrial matrix
      (Reactome:R-HSA-904864).
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "SUBCELLULAR LOCATION: Mitochondrion"
- term:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: >-
      Electronic annotation to the core alanine:glyoxylate transaminase activity
      (EC 2.6.1.44, RHEA:24248), transferred from the rat ortholog. Redundant
      with the IBA/IDA/ISS annotations to the same term.
    action: ACCEPT
    reason: >-
      Correct core molecular function, extensively supported experimentally.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "EC=2.6.1.44"
- term:
    id: GO:0016223
    label: beta-alanine:pyruvate transaminase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: >-
      Electronic annotation to beta-alanine:pyruvate transaminase activity
      (EC 2.6.1.18), part of AGXT2's documented broad substrate specificity
      (transfers the amino group from beta-alanine to pyruvate). Inferred by
      similarity to the rat ortholog Q64565.
    action: ACCEPT
    reason: >-
      A legitimate member of the multifunctional aminotransferase's substrate
      range as annotated in UniProt; not the core namesake activity but a valid
      enzymatic function.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate"
- term:
    id: GO:0030170
    label: pyridoxal phosphate binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      InterPro-based electronic annotation for pyridoxal 5'-phosphate binding.
      AGXT2 is a PLP-dependent class-III aminotransferase with a PLP Schiff-base
      lysine, so cofactor binding is required for catalysis.
    action: ACCEPT
    reason: >-
      Correct cofactor-binding function; UniProt annotates PLP as the cofactor
      and a N6-(pyridoxal phosphate)lysine modified residue. Enabling/secondary
      to the transaminase catalytic activity.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "N6-(pyridoxal phosphate)lysine"
- term:
    id: GO:0047305
    label: (R)-3-amino-2-methylpropionate:pyruvate transaminase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: >-
      Electronic annotation to (R)-3-amino-2-methylpropanoate (D-beta-
      aminoisobutyrate):pyruvate transaminase activity (EC 2.6.1.40). AGXT2 is
      identical to D-3-aminoisobutyrate-pyruvate aminotransferase and metabolises
      the D-isomer of beta-aminoisobutyrate.
    action: ACCEPT
    reason: >-
      Correct; directly demonstrated for the human enzyme (IDA, PMID:24586340)
      and consistent with the UniProt catalytic-activity record.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "D-3-aminoisobutyrate-pyruvate aminotransferase"
- term:
    id: GO:0047635
    label: L-alanine:oxo-acid transaminase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000116
  qualifier: enables
  review:
    summary: >-
      RHEA-mapping electronic annotation to the general L-alanine:oxo-acid
      transaminase activity, covering the several alanine-dependent transamination
      reactions catalysed by AGXT2 (e.g. with 2-oxobutanoate, oxaloacetate,
      methylarginines as acceptors/donors).
    action: ACCEPT
    reason: >-
      A correct, if more general, grouping term consistent with AGXT2's broad
      alanine-dependent transaminase activity documented in UniProt. It captures
      the shared use of L-alanine/pyruvate as the amino donor/acceptor pair.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Reaction=oxaloacetate + L-alanine = L-aspartate + pyruvate"
- term:
    id: GO:0140385
    label: amino acid transaminase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  qualifier: enables
  review:
    summary: >-
      ARBA machine-learning electronic annotation to the parent term amino acid
      transaminase activity. This is a broad grouping term encompassing AGXT2's
      transaminase activities.
    action: ACCEPT
    reason: >-
      Correct but general; the more specific alanine:glyoxylate transaminase and
      other transaminase terms are the informative core annotations. Retained as
      a valid, non-core parent.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Multifunctional aminotransferase with a broad substrate"
- term:
    id: GO:0006545
    label: glycine biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:20018850
  qualifier: involved_in
  review:
    summary: >-
      Direct-assay involvement in glycine biosynthesis: AGXT2 forms glycine from
      glyoxylate by transamination (glyoxylate + L-alanine = glycine + pyruvate).
      Rodionov et al. characterized the human enzyme's function and localization.
    action: ACCEPT
    reason: >-
      Correct; glycine is the product of the namesake reaction. UniProt's DR
      cross-reference uses the more specific child GO:0019265 "glycine
      biosynthetic process, by transamination of glyoxylate", which better
      captures the mechanism, but GO:0006545 is accurate.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Catalyzes the conversion of glyoxylate to glycine using alanine as the"
- term:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  evidence_type: IDA
  original_reference_id: PMID:20018850
  qualifier: enables
  review:
    summary: >-
      Direct experimental demonstration of alanine:glyoxylate transaminase
      activity for human AGXT2. Rodionov et al. cloned and expressed human AGXT2
      and characterized its aminotransferase function.
    action: ACCEPT
    reason: >-
      Core molecular function with direct experimental support in the human
      enzyme.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Multifunctional aminotransferase with a broad substrate specificity"
- term:
    id: GO:0042853
    label: L-alanine catabolic process
  evidence_type: IDA
  original_reference_id: PMID:20018850
  qualifier: involved_in
  review:
    summary: >-
      Direct-assay involvement in L-alanine catabolism, reflecting consumption of
      L-alanine as the amino donor in AGXT2 transaminase reactions.
    action: ACCEPT
    reason: >-
      Consistent with the biochemistry of the alanine:glyoxylate transaminase
      reaction, where L-alanine is deaminated to pyruvate.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Catalyzes the conversion of glyoxylate to glycine using alanine as the"
- term:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: >-
      Sequence-similarity annotation of alanine:glyoxylate transaminase activity
      transferred from the rat ortholog Q64565. Redundant with the human IDA/IBA
      annotations to the same core term.
    action: ACCEPT
    reason: >-
      Correct core molecular function; the human enzyme is directly demonstrated
      to have this activity, so the ISS is well supported.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "EC=2.6.1.44"
- term:
    id: GO:0016223
    label: beta-alanine:pyruvate transaminase activity
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: >-
      Sequence-similarity annotation of beta-alanine:pyruvate transaminase
      activity (EC 2.6.1.18) transferred from the rat ortholog Q64565, part of
      AGXT2's broad substrate range.
    action: ACCEPT
    reason: >-
      A documented reaction of the multifunctional enzyme (UniProt catalytic
      activity, by similarity); valid but non-core.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Beta-alanine-pyruvate aminotransferase"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  qualifier: located_in
  review:
    summary: >-
      High-throughput mitochondrial-proteome study assigning AGXT2 to the
      mitochondrion. Consistent with the directly established mitochondrial
      localization of the enzyme.
    action: ACCEPT
    reason: >-
      Correct localization; corroborates the IDA localization annotations.
    supported_by:
    - reference_id: PMID:34800366
      supporting_text: "high-confidence human mitochondrial proteome"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:31818439
  qualifier: located_in
  review:
    summary: >-
      Direct experimental localization of human AGXT2 to the mitochondrion by
      double immunofluorescence with an anti-mitochondrial antibody in human
      kidney/liver tissue.
    action: ACCEPT
    reason: >-
      Direct experimental support for mitochondrial localization in native human
      tissue.
    supported_by:
    - reference_id: PMID:31818439
      supporting_text: "The double fluorescent staining revealed mitochondrial localization"
- term:
    id: GO:0047305
    label: (R)-3-amino-2-methylpropionate:pyruvate transaminase activity
  evidence_type: IDA
  original_reference_id: PMID:24586340
  qualifier: enables
  review:
    summary: >-
      Direct experimental demonstration that human AGXT2 metabolises
      beta-aminoisobutyrate (D-BAIB), the prototypic AGXT2 substrate, via
      (R)-3-amino-2-methylpropanoate:pyruvate transaminase activity
      (EC 2.6.1.40). Kittel et al. assayed AGXT2 activity using BAIB as
      substrate in HEK cells overexpressing the human enzyme, and the
      p.Val140Ile variant significantly reduced BAIB degradation.
    action: ACCEPT
    reason: >-
      Directly supported enzymatic activity of the human enzyme; BAIB is
      described as a prototypic AGXT2 substrate.
    supported_by:
    - reference_id: PMID:24586340
      supporting_text: "prototypic substrate of AGXT2"
    - reference_id: PMID:24586340
      supporting_text: "significant reduction of enzyme activity was observed"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:24586340
  qualifier: located_in
  review:
    summary: >-
      Direct experimental localization of human AGXT2 to the mitochondrion by
      immunofluorescence with MitoTracker co-staining in HEK cells overexpressing
      the enzyme.
    action: ACCEPT
    reason: >-
      Direct experimental support; consistent with all other localization
      evidence.
    supported_by:
    - reference_id: PMID:24586340
      supporting_text: "AGXT2 was localized to mitochondria in both cell lines"
- term:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  evidence_type: IDA
  original_reference_id: PMID:24586340
  qualifier: enables
  review:
    summary: >-
      Direct experimental demonstration of alanine:glyoxylate transaminase
      activity in human AGXT2. Kittel et al. measured AGXT2 enzyme activity using
      pyruvate and glyoxylate as amino-group acceptor and PLP as cofactor, and
      showed the p.Val140Ile variant reduces this activity.
    action: ACCEPT
    reason: >-
      Core molecular function with direct human experimental support.
    supported_by:
    - reference_id: PMID:24586340
      supporting_text: "1 mM sodium pyruvate and 1 mM sodium glyoxylate as amino group acceptor"
- term:
    id: GO:0005759
    label: mitochondrial matrix
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-904864
  qualifier: located_in
  review:
    summary: >-
      Reactome traceable-author statement localizing the AGXT2 transamination
      reaction to the mitochondrial matrix. Consistent with the enzyme being a
      soluble matrix aminotransferase.
    action: ACCEPT
    reason: >-
      Correct sub-compartment; the mature enzyme is imported into the
      mitochondrial matrix via its cleaved transit peptide.
    supported_by:
    - reference_id: Reactome:R-HSA-904864
      supporting_text: "Mitochondrial AGXT2 (alanine-glyoxylate transaminase 2) catalyzes the irreversible\nreaction of glyoxylate and alanine to form glycine and pyruvate"
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:20018850
  qualifier: located_in
  review:
    summary: >-
      Direct experimental demonstration of mitochondrial localization of human
      AGXT2 by confocal microscopy, with delineation of a 41-amino-acid
      N-terminal mitochondrial cleavage sequence by N-terminal sequencing of the
      mature protein.
    action: ACCEPT
    reason: >-
      Foundational, direct experimental evidence for mitochondrial localization
      of the human enzyme.
    supported_by:
    - reference_id: PMID:20018850
      supporting_text: "Mitochondrial localization of human AGXT2 was demonstrated by"
- term:
    id: GO:0009436
    label: glyoxylate catabolic process
  evidence_type: IDA
  original_reference_id: PMID:20018850
  qualifier: involved_in
  review:
    summary: >-
      Direct-assay involvement in glyoxylate catabolism: AGXT2 converts
      glyoxylate to glycine, consuming glyoxylate.
    action: ACCEPT
    reason: >-
      Correct; the reaction detoxifies glyoxylate by transamination. The IBA
      annotation to the same term is likewise accepted.
    supported_by:
    - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
      supporting_text: "Catalyzes the conversion of glyoxylate to glycine using alanine as the"
- term:
    id: GO:0045429
    label: positive regulation of nitric oxide biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:20018850
  qualifier: involved_in
  review:
    summary: >-
      Direct-assay finding that human AGXT2 overexpression lowers ADMA (an
      endogenous inhibitor of NO synthase) and thereby protects endothelial cells
      from ADMA-mediated inhibition of nitric oxide production. This links AGXT2
      methylarginine metabolism to positive regulation of NO biosynthesis.
    action: KEEP_AS_NON_CORE
    reason: >-
      Well supported physiologically, but this is a downstream regulatory
      consequence of AGXT2's methylarginine-transaminase activity (via lowering
      ADMA), not a direct enzymatic core function. Retain as a non-core
      biological-process annotation.
    supported_by:
    - reference_id: PMID:20018850
      supporting_text: "protected endothelial cells from"
    - reference_id: PMID:20018850
      supporting_text: "decreased ADMA levels and improved endothelial NO production"
core_functions:
- description: >-
    Mitochondrial PLP-dependent aminotransferase that transaminates glyoxylate to
    glycine using L-alanine as amino donor (alanine:glyoxylate transaminase,
    EC 2.6.1.44), contributing to glyoxylate detoxification.
  molecular_function:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  directly_involved_in:
  - id: GO:0009436
    label: glyoxylate catabolic process
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
    supporting_text: "Reaction=glyoxylate + L-alanine = glycine + pyruvate"
  - reference_id: PMID:24586340
    supporting_text: "1 mM sodium pyruvate and 1 mM sodium glyoxylate as amino group acceptor"
- description: >-
    Transaminates D-beta-aminoisobutyrate (a pyrimidine-catabolism end product)
    with pyruvate ((R)-3-amino-2-methylpropanoate:pyruvate transaminase,
    EC 2.6.1.40); AGXT2 activity is the main determinant of urinary
    beta-aminoisobutyrate excretion.
  molecular_function:
    id: GO:0047305
    label: (R)-3-amino-2-methylpropionate:pyruvate transaminase activity
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: PMID:24586340
    supporting_text: "prototypic substrate of AGXT2"
  - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
    supporting_text: "D-3-aminoisobutyrate-pyruvate aminotransferase"
- description: >-
    Broad-specificity amino acid transaminase that also metabolises the
    endogenous NO-synthase inhibitors ADMA and SDMA and other amino-acid
    substrates, using L-alanine/pyruvate as the amino donor/acceptor pair;
    requires pyridoxal 5'-phosphate as cofactor.
  molecular_function:
    id: GO:0008453
    label: L-alanine:glyoxylate transaminase activity
  directly_involved_in:
  - id: GO:0042853
    label: L-alanine catabolic process
  locations:
  - id: GO:0005759
    label: mitochondrial matrix
  supported_by:
  - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
    supporting_text: "Multifunctional aminotransferase with a broad substrate specificity"
  - reference_id: file:human/AGXT2/AGXT2-uniprot.txt
    supporting_text: "N6-(pyridoxal phosphate)lysine"
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000116
  title: Automatic Gene Ontology annotation based on Rhea mapping
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:20018850
  title: Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine
    and protects from inhibition of nitric oxide production.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      PubMed-verified. Establishes human AGXT2 as a mitochondrial enzyme that
      metabolises ADMA and protects endothelial NO production; foundational for
      the localization and methylarginine/NO annotations. Abstract-only in cache;
      localization and NO-protection quotes taken verbatim from the abstract.
- id: PMID:24586340
  title: Alanine-glyoxylate aminotransferase 2 (AGXT2) polymorphisms have considerable
    impact on methylarginine and β-aminoisobutyrate metabolism in healthy volunteers.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      PubMed-verified, full text available. Directly assays human AGXT2 activity
      on BAIB and SDMA and characterizes the activity-reducing p.Val140Ile
      variant; supports the BAIB/methylarginine transaminase and alanine:glyoxylate
      transaminase annotations.
- id: PMID:31818439
  title: Kidney and liver are the main organs of expression of a key metabolic enzyme
    alanine:glyoxylate aminotransferase 2 in humans.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      PubMed-verified. Immunohistochemistry and double immunofluorescence
      establish AGXT2 protein expression in human kidney convoluted tubule and
      liver hepatocytes and its mitochondrial localization.
- id: PMID:34800366
  title: Quantitative high-confidence human mitochondrial proteome and its dynamics
    in cellular context.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      PubMed-verified high-confidence mitochondrial proteome; supports the HTP
      mitochondrion localization. AGXT2 is one of thousands of proteins in the
      dataset, so it is corroborating rather than gene-specific.
- id: Reactome:R-HSA-904864
  title: Mitochondrial AGXT2 tetramer transaminates glyoxylate and alanine to glycine
    and pyruvate
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Reactome reaction for AGXT2 in the mitochondrial matrix; notes that most in
      vivo glyoxylate-to-glycine flux is peroxisomal (AGXT) and the physiological
      role of the AGXT2 reaction is uncertain, useful context for weighting the
      glyoxylate BP annotations.