GLUD1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (PAN-GO) inference of the NAD(+)-dependent glutamate dehydrogenase activity. This is the well-established catalytic activity of GLUD1 and is directly supported by human experimental data. Because GLUD1 is a genuine dual-cofactor enzyme using both NAD(+) and NADP(+), the umbrella term GO:0004353 [NAD(P)+] is the most representative core function; the NAD(+)-specific term is accurate as a component of that activity. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Mitochondrial glutamate dehydrogenase that catalyzes the
GO:0006538 L-glutamate catabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic inference that GLUD1 participates in glutamate catabolism. This is the core biological process the enzyme executes (oxidative deamination of glutamate) and is experimentally supported in human. Supporting Evidence: PMID:6121377 Decreased glutamate
GO:0005739 mitochondrion	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Phylogenetic inference of mitochondrial localization. Correct; the enzyme is predominantly mitochondrial. The more specific and experimentally supported location is the mitochondrial matrix (GO:0005759), so this general term is retained as accurate but non-core. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt translocates into the mitochondria, only a small amount of the protein
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	IEA GO_REF:0000120	ACCEPT	Summary: Automated (ARBA/RHEA) assignment of NAD(+)-dependent glutamate dehydrogenase activity, consistent with EC 1.4.1.3 and the RHEA:15133 reaction listed in UniProt. Accurate and experimentally corroborated. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Reaction=L-glutamate + NAD(+) + H2O = 2-oxoglutarate
GO:0004353 L-glutamate dehydrogenase [NAD(P)+] activity	IEA GO_REF:0000003	ACCEPT	Summary: EC-mapping (EC 1.4.1.3) assignment of the dual-cofactor [NAD(P)+] glutamate dehydrogenase activity. This is the single most representative molecular function of GLUD1, which uses both NAD(+) and NADP(+); it is experimentally supported and designated core. Supporting Evidence: PMID:11254391 only animal GDH utilizes
GO:0004354 L-glutamate dehydrogenase (NADP+) activity	IEA GO_REF:0000116	ACCEPT	Summary: Automated (RHEA:11612) assignment of NADP(+)-dependent glutamate dehydrogenase activity. GLUD1 genuinely uses NADP(+) as well as NAD(+); the NADP(+) reaction is experimentally documented (PMID:11032875) and listed in UniProt. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Reaction=L-glutamate + NADP(+) + H2O = 2-oxoglutarate
GO:0005525 GTP binding	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: ARBA electronic assignment of GTP binding. GTP is the major allosteric inhibitor of GLUD1 and binds a defined regulatory site; this is supported by an experimental IDA annotation (PMID:11032875) and by GTP-binding residues in UniProt. Kept as an accurate regulatory-ligand binding function (non-core). Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Inhibited by GTP and ATP
GO:0005739 mitochondrion	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: UniProt subcellular-location keyword mapping to mitochondrion. Correct and redundant with the experimental IDA mitochondrion annotations; retained as accurate but non-core relative to mitochondrial matrix. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion
GO:0005783 endoplasmic reticulum	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: UniProt subcellular-location keyword mapping to endoplasmic reticulum. This reflects a genuine but minor extramitochondrial pool of GLUD1; it is not the core site of function. Reason: UniProt records the ER location from PMID:19448744 (ECO:0000269), so this row carries the same claim as the IDA row. ORGANELLES check (2026-11-05): the only source is PMID:19448744 (abstract-only in cache), in which overexpressed hGDH1-EGFP in COS 7, HeLa, CHO, HEK293 and SH-SY5Y cells co-localized mainly with DsRed2-Mito and to a lesser extent with the co-transfected marker DsRed2-ER, and a ~95 kDa full-length (presequence-retaining) band fractionated with the ER-containing cytosol. GLUD1 has a mitochondrial presequence, no ER signal peptide, TM segment or retention motif, so any ER pool is on the cytosolic face and stays at the root with no ER membrane or lumen term. The row is kept as a minor non-core pool, as for AHCY in ER batch 1 (overexpressed fusion against an ER marker), deferring to the curator's full-text reading; MARK_AS_OVER_ANNOTATED is a close alternative, since the ER signal comes only from overexpressed, tagged, unprocessed precursor and could be a targeting artefact. Supporting Evidence: PMID:19448744 part of the protein localizes to the endoplasmic reticulum file:human/GLUD1/GLUD1-uniprot.txt Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum. PMID:19448744 colocalized with the mitochondrial marker DsRed2-Mito and to a lesser extent with the endoplasmic reticulum marker DsRed2-ER
GO:0006520 amino acid metabolic process	IEA GO_REF:0000002	MODIFY	Summary: InterPro2GO assignment of a very general amino-acid metabolic process. GLUD1 indeed acts in amino-acid (glutamate) metabolism, but the specific, better term is L-glutamate catabolic process (GO:0006538), which is already annotated experimentally. This general term should be replaced by the specific one. Proposed replacements: L-glutamate catabolic process Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt catalyzes the
GO:0006538 L-glutamate catabolic process	IEA GO_REF:0000117	ACCEPT	Summary: ARBA electronic assignment of glutamate catabolism, redundant with the experimental IDA/IBA annotations to the same term. Accurate core process. Supporting Evidence: PMID:11903050 catalyses the reversible oxidative deamination of l-glutamate to 2-oxoglutarate in the mitochondrial matrix
GO:0016491 oxidoreductase activity	IEA GO_REF:0000002	MODIFY	Summary: InterPro2GO high-level oxidoreductase activity. Correct but far too general; the specific catalytic function is L-glutamate dehydrogenase [NAD(P)+] activity (GO:0004353), which is annotated experimentally. Replace with the specific term. Proposed replacements: L-glutamate dehydrogenase [NAD(P)+] activity Supporting Evidence: PMID:11254391 oxidative
GO:0016639 oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor	IEA GO_REF:0000002	MODIFY	Summary: InterPro2GO assignment of the parent class of amino-acid dehydrogenase activity. Accurate but a generalization of the specific glutamate dehydrogenase [NAD(P)+] activity (GO:0004353). Replace with the specific term. Proposed replacements: L-glutamate dehydrogenase [NAD(P)+] activity Supporting Evidence: PMID:11254391 deamination of l-glutamate to 2-oxoglutarate
GO:0043531 ADP binding	IEA GO_REF:0000117	ACCEPT	Summary: ARBA electronic assignment of ADP binding, redundant with the experimental IDA ADP-binding annotation (PMID:12742085). ADP is the principal allosteric activator of GLUD1 and binds a defined site; this is a core regulatory-ligand binding function. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Activated by ADP
GO:0070728 L-leucine binding	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: ARBA electronic assignment of L-leucine binding, redundant with the experimental IDA annotation (PMID:12742085). L-leucine is a physiological allosteric activator of GLUD1; accurate regulatory function (non-core). Supporting Evidence: PMID:11032875 L-leucine, at 1.0 mM:, enhanced the activity of the nerve tissue-specific
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	REMOVE	Summary: Generic protein binding from a high-throughput affinity-purification interactome (BioPlex). The term is uninformative about GLUD1 molecular function; the recorded partners (GLUD2 paralog, KLHL22) are captured elsewhere. Removed per curation policy for bare protein binding IPIs.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	REMOVE	Summary: Generic protein binding from a large-scale interactome (BioPlex 3.0). Uninformative molecular-function term; removed.
GO:0005515 protein binding	IPI PMID:37788672 Cryo-EM structure of the KLHL22 E3 ligase bound to an oligom...	REMOVE	Summary: Protein binding from the cryo-EM structure of the KLHL22 E3 ligase bound to the GDH1 hexamer. Although this is a biologically meaningful interaction (KLHL22/CUL3 ubiquitinates GDH1), the bare protein binding term is uninformative; the specific relationship is documented in the notes and the KLHL22 interaction is retained in UniProt. Bare protein binding removed. Supporting Evidence: PMID:37788672 ligase mediated the polyubiquitination of GDH1 in vitro
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	REMOVE	Summary: Generic protein binding from a multimodal cell-map/interactome study. Uninformative molecular-function term; removed.
GO:0005739 mitochondrion	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: Immunofluorescence (HPA) localization to mitochondrion. Correct; consistent with the predominant mitochondrial localization. Retained as accurate but non-core relative to mitochondrial matrix.
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	EXP PMID:11254391 Structures of bovine glutamate dehydrogenase complexes eluci...	ACCEPT	Summary: Experimental characterization of GDH catalytic activity and purine regulation from crystallographic/kinetic studies (bovine GDH structures; human HHS mutant kinetics). Supports the NAD(+)-dependent glutamate dehydrogenase activity of GLUD1. Core catalytic function. Supporting Evidence: PMID:11254391 deamination of l-glutamate to 2-oxoglutarate
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	EXP PMID:16023112 Identification of ADP-ribosylation site in human glutamate d...	ACCEPT	Summary: Experimental measurement of purified human GDH activity and its inhibition by ADP-ribosylation. Confirms the NAD(+)-dependent glutamate dehydrogenase activity of GLUD1. Core catalytic function. Supporting Evidence: PMID:16023112 hGDH isozymes were inhibited by up to 75%
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	EXP PMID:16959573 SIRT4 inhibits glutamate dehydrogenase and opposes the effec...	ACCEPT	Summary: Experimental demonstration that GDH activity is regulated (downregulated by SIRT4-mediated ADP-ribosylation). Supports the NAD(+)-dependent glutamate dehydrogenase activity. Core catalytic function. Supporting Evidence: PMID:16959573 downregulate glutamate dehydrogenase (GDH) activity
GO:0004354 L-glutamate dehydrogenase (NADP+) activity	EXP PMID:11032875 Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human...	ACCEPT	Summary: Experimental kinetic characterization of recombinant human GLUD1-derived GDH, which functions with NADP(+) as well as NAD(+). Supports the NADP(+)-dependent activity, part of the dual-cofactor core function. Supporting Evidence: PMID:11032875 Nonactivated GLUD1 GDH was markedly inhibited
GO:0005739 mitochondrion	HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an...	KEEP AS NON CORE	Summary: High-throughput mitochondrial-proteome detection. Consistent with the established mitochondrial localization; accurate but non-core relative to mitochondrial matrix.
GO:0042803 protein homodimerization activity	IPI PMID:11903050 Expression, purification and characterization of human gluta...	KEEP AS NON CORE	Summary: Self-interaction annotation. GLUD1 assembles into a homohexamer (a trimer of dimers), so a homo-oligomerization/self-association activity is real, though homodimerization is a slightly imprecise description of the hexameric assembly. The self-association is intrinsic to enzyme assembly rather than a standalone signaling function, so it is kept as non-core. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Homohexamer (By similarity)
GO:0005739 mitochondrion	IDA PMID:19448744 Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mi...	KEEP AS NON CORE	Summary: Experimental (confocal colocalization with a mitochondrial marker) localization to mitochondrion. Directly supports the predominant mitochondrial localization of GLUD1. Retained as accurate but non-core relative to the matrix term. Supporting Evidence: PMID:19448744 colocalized with the mitochondrial marker DsRed2-Mito
GO:0005783 endoplasmic reticulum	IDA PMID:19448744 Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mi...	KEEP AS NON CORE	Summary: Experimental colocalization showing a minor pool of GLUD1 in the endoplasmic reticulum in addition to mitochondria. Real but minor; not the core site of function. Reason: ORGANELLES check (2026-11-05): the only source is PMID:19448744 (abstract-only in cache), in which overexpressed hGDH1-EGFP in COS 7, HeLa, CHO, HEK293 and SH-SY5Y cells co-localized mainly with DsRed2-Mito and to a lesser extent with the co-transfected marker DsRed2-ER, and a ~95 kDa full-length (presequence-retaining) band fractionated with the ER-containing cytosol. GLUD1 has a mitochondrial presequence, no ER signal peptide, TM segment or retention motif, so any ER pool is on the cytosolic face and stays at the root with no ER membrane or lumen term. The row is kept as a minor non-core pool, as for AHCY in ER batch 1 (overexpressed fusion against an ER marker), deferring to the curator's full-text reading; MARK_AS_OVER_ANNOTATED is a close alternative, since the ER signal comes only from overexpressed, tagged, unprocessed precursor and could be a targeting artefact. Supporting Evidence: PMID:19448744 part of the protein localizes to the endoplasmic reticulum file:human/GLUD1/GLUD1-uniprot.txt Mostly translocates into the mitochondria, only a small amount of the protein localizes to the endoplasmic reticulum. PMID:19448744 colocalized with the mitochondrial marker DsRed2-Mito and to a lesser extent with the endoplasmic reticulum marker DsRed2-ER
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-5688276	ACCEPT	Summary: Reactome traceable-author localization to the mitochondrial matrix (in the context of SIRT4 transferring ADP-ribose to GLUD). This is the specific, correct site of the active enzyme. Core location. Supporting Evidence: PMID:11903050 in the mitochondrial matrix
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-5688289	ACCEPT	Summary: Reactome traceable-author localization to the mitochondrial matrix (SIRT3 deacetylation reaction context). Correct core location of the enzyme. Supporting Evidence: PMID:11903050 in the mitochondrial matrix
GO:0021762 substantia nigra development	HEP PMID:22926577 Quantitative proteomic analysis of human substantia nigra in...	MARK AS OVER ANNOTATED	Summary: Derived from a quantitative proteomics survey of human substantia nigra in neurodegenerative disease (expression-pattern HEP evidence). Mere detection or differential abundance in a brain region does not establish a role in substantia nigra development; this is an over-annotation of GLUD1 function.
GO:0006541 L-glutamine metabolic process	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Sequence-similarity transfer of a role in glutamine metabolism. GLUD1 does not act directly on glutamine, but it is central to glutamine anaplerosis by producing alpha-ketoglutarate downstream of glutaminase; this places it within the glutamine metabolic network. Kept as accurate but non-core (indirect). Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt glutamine anaplerosis by producing alpha-ketoglutarate, an important
GO:0072350 tricarboxylic acid metabolic process	ISS GO_REF:0000024	ACCEPT	Summary: Sequence-similarity transfer of a role in TCA-cycle intermediate metabolism. Accurate: GLUD1 supplies alpha-ketoglutarate, a key TCA intermediate, linking it to the tricarboxylic acid metabolic process (anaplerosis). Core-adjacent process reflecting the enzyme principal metabolic role. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt intermediate in the tricarboxylic acid cycle
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-70589	ACCEPT	Summary: Reactome traceable-author localization to the mitochondrial matrix, annotated on the reverse GDH reaction (alpha-ketoglutarate + NH4+ + NAD(P)H -> glutamate). Correct core location. Supporting Evidence: PMID:11903050 in the mitochondrial matrix
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-70600	ACCEPT	Summary: Reactome traceable-author localization to the mitochondrial matrix, annotated on the forward GDH reaction (glutamate + NAD(P)+ -> alpha-ketoglutarate). Correct core location. Supporting Evidence: PMID:11903050 in the mitochondrial matrix
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-9838081	ACCEPT	Summary: Reactome traceable-author localization to the mitochondrial matrix (LONP1 degradation of matrix proteins context). Correct core location. Supporting Evidence: PMID:11903050 in the mitochondrial matrix
GO:0005759 mitochondrial matrix	TAS Reactome:R-HSA-9838093	ACCEPT	Summary: Reactome traceable-author localization to the mitochondrial matrix (LONP1 binding of matrix proteins context). Correct core location. Supporting Evidence: PMID:11903050 in the mitochondrial matrix
GO:0005515 protein binding	IPI PMID:16959573 SIRT4 inhibits glutamate dehydrogenase and opposes the effec...	REMOVE	Summary: Protein binding annotation with SIRT4 (Q9Y6E7) as partner. The biologically meaningful relationship is that SIRT4 ADP-ribosylates and inhibits GLUD1; the bare protein binding term is uninformative about the GLUD1 molecular function. Removed per policy. Supporting Evidence: PMID:16959573 SIRT4 is a mitochondrial enzyme that uses NAD to ADP-ribosylate
GO:0070728 L-leucine binding	IDA PMID:12742085 Study of structure-function relationships in human glutamate...	KEEP AS NON CORE	Summary: Experimental (structure-function/mutagenesis) evidence for L-leucine binding, the physiological allosteric activator site. Accurate regulatory-ligand binding function; kept as non-core relative to catalysis. Supporting Evidence: PMID:11032875 L-leucine, at 1.0 mM:, enhanced the activity of the nerve tissue-specific
GO:0005525 GTP binding	IDA PMID:11032875 Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human...	KEEP AS NON CORE	Summary: Experimental evidence for GTP binding, the major allosteric inhibitor of GLUD1 (nonactivated enzyme inhibited by GTP with IC50 ~0.2 microM). Accurate regulatory-ligand binding function; central to physiology and disease (loss of GTP inhibition causes HHF6) but kept as non-core relative to catalysis. Supporting Evidence: PMID:11032875 Nonactivated GLUD1 GDH was markedly inhibited
GO:0005737 cytoplasm	IDA PMID:18688271 Mitochondrial targeting adaptation of the hominoid-specific ...	KEEP AS NON CORE	Summary: Experimental localization showing GLUD1 in the cytoplasm in addition to mitochondria (in contrast to the mitochondria-specific GLUD2). This is a genuine but minor extramitochondrial pool; not the core site of function. Supporting Evidence: PMID:18688271 GLUD1 localizes to the mitochondria as well as the cytoplasm
GO:0043531 ADP binding	IDA PMID:12742085 Study of structure-function relationships in human glutamate...	ACCEPT	Summary: Experimental (structure-function) evidence for ADP binding, the principal allosteric activator site of GLUD1. ADP binding is core to the activated physiological state of the enzyme. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Activated by ADP
GO:0097054 L-glutamate biosynthetic process	IDA PMID:11032875 Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human...	KEEP AS NON CORE	Summary: The GDH reaction is reversible, and in the reductive amination direction (alpha-ketoglutarate + NH4+ + NAD(P)H -> glutamate) GLUD1 can synthesize glutamate. Reactome models this reverse reaction (R-HSA-70589). Real capacity, but the physiologically dominant/core direction is oxidative deamination (catabolic); glutamate biosynthesis is kept as non-core. Supporting Evidence: file:human/GLUD1/GLUD1-uniprot.txt Reaction=L-glutamate + NAD(+) + H2O = 2-oxoglutarate
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	IDA PMID:11903050 Expression, purification and characterization of human gluta...	ACCEPT	Summary: Direct experimental characterization of purified recombinant human GDH (wild-type and allosteric-regulatory mutants), confirming NAD(+)-dependent glutamate dehydrogenase activity. Core catalytic function. Supporting Evidence: PMID:11903050 catalyses the reversible oxidative deamination of l-glutamate to 2-oxoglutarate in the mitochondrial matrix
GO:0004353 L-glutamate dehydrogenase [NAD(P)+] activity	IDA PMID:11032875 Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human...	ACCEPT	Summary: Direct experimental evidence for the dual-cofactor [NAD(P)+] glutamate dehydrogenase activity of human GLUD1-derived GDH. This is the single most representative molecular function of the gene. Core catalytic function. Supporting Evidence: PMID:11254391 only animal GDH utilizes
GO:0006538 L-glutamate catabolic process	IDA PMID:11032875 Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human...	ACCEPT	Summary: Direct experimental support for GLUD1 role in glutamate catabolism (oxidative deamination). Core biological process. Supporting Evidence: PMID:11903050 catalyses the reversible oxidative deamination of l-glutamate to 2-oxoglutarate in the mitochondrial matrix
GO:0032024 positive regulation of insulin secretion	IMP PMID:11502802 Acute insulin responses to leucine in children with the hype...	KEEP AS NON CORE	Summary: Clinical/mutation evidence that GLUD1 activity promotes insulin secretion: gain-of-function GLUD1 mutations (loss of GTP inhibition) cause exaggerated leucine-stimulated insulin release in the hyperinsulinism/hyperammonemia syndrome. This is a genuine, physiologically and clinically important role in pancreatic beta-cells, but it is a downstream, tissue-specific function rather than the enzyme core catalytic role. Kept as non-core. Supporting Evidence: PMID:11502802 syndrome by desensitizing glutamate dehydrogenase to allosteric inhibition by
GO:0070403 NAD+ binding	IDA PMID:12193607 Importance of glutamate 279 for the coenzyme binding of huma...	KEEP AS NON CORE	Summary: Direct experimental identification of the NAD(+) coenzyme-binding site (photoaffinity labeling and mutagenesis of Glu279). NAD(+) binding is intrinsic to catalysis; a genuine cofactor-binding function, kept as non-core relative to the catalytic activity term it supports. Supporting Evidence: PMID:12193607 Glu(279) plays an important role for efficient binding of NAD(+) to human
GO:0004352 L-glutamate dehydrogenase (NAD+) activity	IDA PMID:15578726 Molecular basis of human glutamate dehydrogenase regulation ...	ACCEPT	Summary: Direct experimental characterization of recombinant human GLUD1-derived GDH activity and its regulation. Confirms NAD(+)-dependent glutamate dehydrogenase activity. Core catalytic function. Supporting Evidence: PMID:15578726 GTP potently inhibits GLUD1-derived GDH
GO:0005739 mitochondrion	IDA PMID:15578726 Molecular basis of human glutamate dehydrogenase regulation ...	KEEP AS NON CORE	Summary: Experimental (GFP-fusion imaging) localization of GLUD1 to mitochondria, colocalizing with a mitochondrial marker. Supports the predominant mitochondrial localization; kept as non-core relative to mitochondrial matrix. Supporting Evidence: PMID:15578726 revealed a GFP fluorescence pattern nearly identical to that of the
GO:0006538 L-glutamate catabolic process	IDA PMID:6121377 Abnormal glutamate metabolism in an adult-onset degenerative...	ACCEPT	Summary: Human evidence linking GDH deficiency to impaired glutamate catabolism (elevated plasma glutamate, reduced alpha-ketoglutarate; decreased glutamate catabolism in patients with partial GDH deficiency). Supports the core glutamate catabolic process. Supporting Evidence: PMID:6121377 Decreased glutamate

Gene Description

Existing Annotations Review

Core Functions

ADP binding: binds ADP at a defined allosteric site, which activates the enzyme (and sensitizes it to L-leucine). ADP binding drives GLUD1 into its catalytically active state under conditions of high ADP:ATP ratio, integrating enzyme activity with cellular energy charge.

References

Deep Research

Falcon

📚 Additional Documentation

Notes

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