Glyceraldehyde-3-phosphate dehydrogenase 1 (Tdh1, YJL052W) is one of three paralogous NAD+-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenases (GAPDH, EC 1.2.1.12; TDH1, TDH2, TDH3) of Saccharomyces cerevisiae. These homotetrameric enzymes catalyse the reversible oxidative phosphorylation of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate with reduction of NAD+ to NADH, the sixth step of glycolysis and an obligatory step of gluconeogenesis. Tdh1 is the minor isoform, contributing about 10-15% of cellular GAPDH activity in exponentially growing cells; its expression rises in stationary phase, on glucose starvation and after heat shock, and the polypeptide is readily detected only in stationary-phase cells. Tdh1 is cytosolic, and like its paralogs is also found in cell-wall extracts, with minor pools co-purifying with mitochondria and lipid particles. A slow NAD(P)H-hydratase side activity is recorded for yeast GAPDH. During alcoholic fermentation S. cerevisiae secretes GAPDH-derived peptides that act as antimicrobial agents against wine-related yeasts and bacteria; these fragments are shared by the TDH1-3 products.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA from GAPDH node PTN000089475, seeded by the three yeast TDH paralogs among other experimentally characterised GAPDHs. TDH1 is an active NAD-dependent phosphorylating GAPDH, so the inherited activity is correct; TDH1 appearing among the donors reflects its own experimental grounding. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 The contribution of the TDH1, TDH2, and TDH3 gene products to the total glyceraldehyde-3-phosphate dehydrogenase activity in wild type cells is 10-15, 25-30, and 50-60%, respectively |
| GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | IDA PMID:3905788 Differential expression of the three yeast glyceraldehyde-3-... | ACCEPT | Summary: McAlister and Holland used tdh insertion mutants to partition total GAPDH activity among the three genes; TDH1 encodes the minor (10-15%) isoform of cellular GAPDH activity and the authors conclude all three genes encode catalytically active enzyme. Supporting Evidence: PMID:3905788 The contribution of the TDH1, TDH2, and TDH3 gene products to the total glyceraldehyde-3-phosphate dehydrogenase activity in wild type cells is 10-15, 25-30, and 50-60%, respectively PMID:3905788 These data confirm that the three yeast glyceraldehyde-3-phosphate dehydrogenase genes encode catalytically active enzyme |
| GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | IEA GO_REF:0000120 | ACCEPT | Summary: EC 1.2.1.12 / RHEA:10300 mapping from the UniProt catalytic-activity annotation; correct for TDH1. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 These data confirm that the three yeast glyceraldehyde-3-phosphate dehydrogenase genes encode catalytically active enzyme |
| GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (GLUCFERMEN-PWY, superpathway of glucose fermentation) assigning the reversible GAP + NAD+ + Pi <-> 1,3-bisphosphoglycerate step (EC 1.2.1.12) to TDH1; the activity is experimentally established for TDH1. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 These data confirm that the three yeast glyceraldehyde-3-phosphate dehydrogenase genes encode catalytically active enzyme |
| GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (GLUCONEO-PWY-1, gluconeogenesis I) assigning the reversible GAP + NAD+ + Pi <-> 1,3-bisphosphoglycerate step (EC 1.2.1.12) to TDH1; the activity is experimentally established for TDH1. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 These data confirm that the three yeast glyceraldehyde-3-phosphate dehydrogenase genes encode catalytically active enzyme |
| GO:0004365 glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (GLYCOLYSIS, glycolysis I) assigning the reversible GAP + NAD+ + Pi <-> 1,3-bisphosphoglycerate step (EC 1.2.1.12) to TDH1; the activity is experimentally established for TDH1. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 These data confirm that the three yeast glyceraldehyde-3-phosphate dehydrogenase genes encode catalytically active enzyme |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping (SL-0086 Cytoplasm); correct for TDH1, which is detected in cytosolic extracts. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | KEEP AS NON CORE | Summary: High-throughput mitochondrial proteomics detected TDH1 in purified mitochondria. Abundant glycolytic enzymes are frequent co-purifying passengers of mitochondrial preparations, although a genuine outer-surface pool exists (PMID:16962558). Reason: HTP proteomic detection; peripheral, non-core. Supporting Evidence: PMID:24769239 we performed an overall quantitative proteomic and phosphoproteomic study of isolated mitochondria extracted from yeast grown on fermentative (glucose or galactose) and respiratory (lactate) media PMID:16962558 we show that all glycolytic enzymes are associated with mitochondria in yeast |
| GO:0005739 mitochondrion | IDA PMID:16962558 Enolase takes part in a macromolecular complex associated to... | KEEP AS NON CORE | Summary: Brandina et al. report that all glycolytic enzyme activities, including GAPDH, are partly associated with purified mitochondria and that glycolytic enzymes co-purify with an enolase-containing complex at the mitochondrial surface. This is a peripheral association of a small pool of TDH1; the abstract does not resolve individual TDH isoforms, but the curator had full text. Reason: Experimental, not removed; peripheral pool, not the site of core glycolytic activity. Supporting Evidence: PMID:16962558 we show that all glycolytic enzymes are associated with mitochondria in yeast PMID:16962558 The identified components included additional glycolytic enzymes |
| GO:0005739 mitochondrion | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA mapping to mitochondrion for GAPDH. Consistent with experimental detection of a peripheral (outer-surface) mitochondria-associated pool of GAPDH, but this is condition-dependent and not the site of core activity. Reason: Peripheral location propagated electronically; non-core. Supporting Evidence: PMID:16962558 we show that all glycolytic enzymes are associated with mitochondria in yeast |
| GO:0005739 mitochondrion | IPI PMID:16962558 Enolase takes part in a macromolecular complex associated to... | KEEP AS NON CORE | Summary: IPI with ENO2: Brandina et al. co-immunoprecipitated glycolytic enzymes with anti-enolase antibodies from mitochondria, placing GAPDH in an enolase-containing complex on the mitochondrial surface. IPI is an unusual code for a location, but the observation supports a peripheral mitochondria-associated pool. Reason: Experimental, peripheral mitochondrial association; non-core. Supporting Evidence: PMID:16962558 enolase takes part in a large macromolecular complex associated to mitochondria PMID:16962558 The identified components included additional glycolytic enzymes |
| GO:0005739 mitochondrion | IPI PMID:16962558 Enolase takes part in a macromolecular complex associated to... | KEEP AS NON CORE | Summary: IPI with ENO1: Brandina et al. co-immunoprecipitated glycolytic enzymes with anti-enolase antibodies from mitochondria, placing GAPDH in an enolase-containing complex on the mitochondrial surface. IPI is an unusual code for a location, but the observation supports a peripheral mitochondria-associated pool. Reason: Experimental, peripheral mitochondrial association; non-core. Supporting Evidence: PMID:16962558 enolase takes part in a large macromolecular complex associated to mitochondria PMID:16962558 The identified components included additional glycolytic enzymes |
| GO:0005811 lipid droplet | IDA PMID:10515935 Identification and characterization of major lipid particle ... | KEEP AS NON CORE | Summary: Athenstaedt et al. identified GAPDH by MS as a minor component in a gel band of highly purified lipid particles (less abundant than Yju3p). A minor co-purifying pool of an abundant cytosolic enzyme; no role at lipid droplets is described. Reason: Experimental but minor co-fractionation; non-core. Supporting Evidence: PMID:10515935 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Yju3p (the amount of Yju3p was greater than GAPDH) |
| GO:0005811 lipid droplet | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA rule propagating lipid droplet location to GAPDHs, derived from proteomic detection of GAPDH in lipid-particle fractions; consistent with the experimental row but a minor co-fractionating pool, not a characteristic location. Reason: Minor co-fractionation location; non-core. Supporting Evidence: PMID:10515935 glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and Yju3p (the amount of Yju3p was greater than GAPDH) |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: SWAT-GFP library imaging (Meurer/Weill et al.) assigned TDH1 to the cytosol; consistent with its glycolytic role. Supporting Evidence: PMID:26928762 we only assigned localizations that could be easily discriminated by eye: ER, nuclear periphery, cytosol, cell periphery, vacuole lumen, vacuole membrane, mitochondria, nucleus, bud/bud neck and punctate |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA is_active_in cytosol for glycolytic GAPDHs; correct for TDH1. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts |
| GO:0005829 cytosol | IDA PMID:11158358 The glyceraldehyde-3-phosphate dehydrogenase polypeptides en... | ACCEPT | Summary: Delgado et al. detected Tdh1 polypeptide by Western blot in cytosolic extracts of stationary-phase cells; cytosol is the site of GAPDH activity. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA mapping to cytosol; correct for TDH1. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA is_active_in cytosol for the GAPDH step of superpathway of glucose fermentation; TDH1 is a soluble cytosolic glycolytic/gluconeogenic enzyme. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA is_active_in cytosol for the GAPDH step of gluconeogenesis I; TDH1 is a soluble cytosolic glycolytic/gluconeogenic enzyme. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA is_active_in cytosol for the GAPDH step of glycolysis I; TDH1 is a soluble cytosolic glycolytic/gluconeogenic enzyme. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in |
| GO:0005886 plasma membrane | HDA PMID:16622836 The plasma membrane proteome of Saccharomyces cerevisiae and... | KEEP AS NON CORE | Summary: Delom et al. identified ~90 proteins in a stripped plasma-membrane fraction by IEC/LDS-PAGE MS, including TDH1. Abundant glycolytic enzymes are common contaminants of membrane fractions, although yeast GAPDH is also found at the cell surface/cell wall (PMID:11158358). Reason: HTP proteomic detection; plausible peripheral pool, non-core. Supporting Evidence: PMID:16622836 Proteins from a stripped plasma membrane fraction were solubilized with the neutral and non-denaturing detergent, the n-dodecyl beta-D-maltoside. PMID:11158358 By immunoelectron microscopy, the GAPDH protein was detected at the outer surface of the cell wall of wild-type cells, as well as in the cytoplasm |
| GO:0006006 glucose metabolic process | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro IPR006424 (type I GAPDH) mapping to glucose metabolic process. Correct but very general; the specific processes glycolysis and gluconeogenesis are annotated separately. Reason: Correct, general parent-level process; redundant with glycolysis/gluconeogenesis. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in |
| GO:0006094 gluconeogenesis | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA mapping to gluconeogenesis. GAPDH catalyses the reversible step used in both glycolysis and gluconeogenesis, and TDH1 is expressed on ethanol as well as glucose. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 The relative proportions of expression of each gene is the same in cells grown in the presence of glucose or ethanol as carbon source |
| GO:0006094 gluconeogenesis | IEP PMID:3905788 Differential expression of the three yeast glyceraldehyde-3-... | ACCEPT | Summary: McAlister and Holland measured TDH1 expression/activity in ethanol-grown (gluconeogenic) as well as glucose-grown cells. IEP is weak evidence for participation, but the reversible GAPDH step is an obligatory part of gluconeogenesis, so the process assignment is correct. Supporting Evidence: PMID:3905788 The relative proportions of expression of each gene is the same in cells grown in the presence of glucose or ethanol as carbon source |
| GO:0006094 gluconeogenesis | RCA GO_REF:0000123 | ACCEPT | Summary: YeastPathways RCA (gluconeogenesis I) for TDH1; the GAPDH step operates in the gluconeogenic direction during growth on non-fermentable carbon sources. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 The relative proportions of expression of each gene is the same in cells grown in the presence of glucose or ethanol as carbon source |
| GO:0006096 glycolysis | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for glycolysis from the GAPDH clade; TDH1 contributes the minor (10-15%) isoform of the glycolytic GAPDH activity. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:3905788}. PMID:3905788 The contribution of the TDH1, TDH2, and TDH3 gene products to the total glyceraldehyde-3-phosphate dehydrogenase activity in wild type cells is 10-15, 25-30, and 50-60%, respectively |
| GO:0006096 glycolysis | IEA GO_REF:0000120 | ACCEPT | Summary: UniPathway UPA00109 / ARBA mapping to glycolysis; correct for TDH1. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:3905788}. |
| GO:0006096 glycolysis | IEP PMID:3905788 Differential expression of the three yeast glyceraldehyde-3-... | ACCEPT | Summary: McAlister and Holland: total GAPDH activity is 2-fold higher in glucose-grown cells, and TDH1 supplies the minor (10-15%) isoform of it. IEP is indirect, but the glycolytic role of TDH1 is well established. Supporting Evidence: PMID:3905788 The contribution of the TDH1, TDH2, and TDH3 gene products to the total glyceraldehyde-3-phosphate dehydrogenase activity in wild type cells is 10-15, 25-30, and 50-60%, respectively PMID:3905788 The relative proportions of expression of each gene is the same in cells grown in the presence of glucose or ethanol as carbon source |
| GO:0009277 fungal-type cell wall | IDA PMID:11158358 The glyceraldehyde-3-phosphate dehydrogenase polypeptides en... | KEEP AS NON CORE | Summary: Delgado et al. detected catalytically active GAPDH at the outer surface of the cell wall by immunofluorescence, immuno-EM and Western blotting of cell-wall extracts; TDH1 polypeptide was specifically detected in cell-wall extracts. Reason: Experimentally supported secondary (moonlighting) location; function there unknown. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts PMID:11158358 By immunoelectron microscopy, the GAPDH protein was detected at the outer surface of the cell wall of wild-type cells, as well as in the cytoplasm |
| GO:0009277 fungal-type cell wall | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA mapping to fungal-type cell wall; consistent with direct experimental detection of TDH1 in cell-wall extracts. Reason: Secondary location, non-core. Supporting Evidence: PMID:11158358 Tdh1 is only detected in stationary-phase cells, again in both cytosol and cell wall extracts |
| GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor | IEA GO_REF:0000002 | MODIFY | Summary: InterPro GAPDH signatures mapped to the generic parent oxidoreductase activity acting on aldehyde/oxo donors with NAD(P) acceptor. Correct but uninformative; the specific child term GAPDH (NAD+) (phosphorylating) activity is supported. Reason: Too general; replace with the specific activity. Proposed replacements: glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in PMID:3905788 These data confirm that the three yeast glyceraldehyde-3-phosphate dehydrogenase genes encode catalytically active enzyme |
| GO:0019658 bifid shunt | RCA GO_REF:0000123 | REMOVE | Summary: YeastPathways RCA from GLUCFERMEN-PWY mapped to GO bifid shunt, the Bifidobacterium phosphoketolase pathway converting glucose to lactate and acetate. S. cerevisiae has no bifid shunt; TDH1 acts in glycolysis/alcoholic fermentation. Reason: Mis-mapped pathway: bifid shunt does not occur in S. cerevisiae. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:3905788}. |
| GO:0050661 NADP binding | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: InterPro IPR006424 (type I GAPDH family, which includes NADP-dependent plant/cyanobacterial GapB/GapC) mapped to NADP binding. Yeast TDH1 is the NAD+-specific phosphorylating GAPDH (EC 1.2.1.12); the only NADP(H) interaction recorded is a slow NAD(P)H-hydratase side activity, so NADP binding is not a meaningful functional description. Reason: Family-level mapping that over-states cofactor specificity of an NAD-dependent GAPDH. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt FUNCTION: As a side activity, catalyzes the hydration of the file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in |
| GO:0051287 NAD binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: InterPro GAPDH NAD(P)-binding domain mapped to NAD binding; correct, NAD+ is the cosubstrate of TDH1. Part of the catalytic activity rather than a separate function. Reason: Cosubstrate binding; non-core. Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in |
| GO:0061620 obsolete glycolytic process through glucose-6-phosphate | RCA GO_REF:0000123 | MODIFY | Summary: YeastPathways RCA (GLYCOLYSIS) to glycolytic process through glucose-6-phosphate, now obsolete and replaced by glycolysis (GO:0006096). TDH1 does act in glycolysis. Reason: Obsolete term; use replaced_by GO:0006096. Proposed replacements: glycolysis Supporting Evidence: file:yeast/TDH1/TDH1-uniprot.txt glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:3905788}. |
| GO:1904408 melatonin binding | IDA PMID:31708896 Glycolytic Proteins Interact With Intracellular Melatonin in... | MARK AS OVER ANNOTATED | Summary: Morcillo-Parra et al. immunopurified melatonin-associated proteins from fermenting cells with anti-melatonin IgG beads and identified Tdh1/2/3 by MS in one gel band. This is an affinity co-purification without a defined binding site, stoichiometry or physiological effect on TDH1. Reason: Affinity co-purification of abundant GAPDH paralogs is weak support for a specific melatonin-binding activity; the experimental report is retained but likely overstates a physiologic molecular function. Supporting Evidence: PMID:31708896 Surprisingly, most of the proteins identified participate in the glycolytic pathway: pyruvate kinase 1 (Pyk2p; band a), enolase (Eno1p, Eno2p; band c), fructose biphosphate aldolase (Fba1p; band d), and glyceraldehyde-3-phosphate dehydrogenase (Tdh1p, Tdh2p, Tdh3p; band f). PMID:31708896 We subsequently performed immunopurification melatonin-IgG-Dynabeads and identified a set of proteins that interact with melatonin inside the cell. |
| GO:1904408 melatonin binding | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: ARBA rule propagating melatonin binding to GAPDHs, derived from a single affinity pull-down study in yeast that did identify this protein; physiological significance is unknown. Reason: ARBA propagates the same weak affinity-capture result as a molecular-function assertion; the interaction lacks a binding constant, site, or demonstrated physiologic effect. Supporting Evidence: PMID:31708896 We subsequently performed immunopurification melatonin-IgG-Dynabeads and identified a set of proteins that interact with melatonin inside the cell. |
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Download this section (compressed HTML)Q: Does stationary-phase Tdh1 have a distinct role (e.g. in quiescence or stress survival) beyond supplementing GAPDH activity, given that its expression is uncoupled from Tdh2/Tdh3?
Experiment: Compare chronological lifespan and stress survival of tdh1 single mutants and strains in which TDH1 is replaced by TDH2/TDH3 coding sequence under the TDH1 promoter, to test isoform-specific versus dosage roles.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), isozyme 1; involved in glycolysis and gluconeogenesis; tetramer that catalyzes the reaction of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate; detected in the cytoplasm and cell wall; protein abundance increases in response to DNA replication stress; GAPDH-derived antimicrobial peptides secreted by S. cerevisiae are active against a wide variety of wine-related yeasts and bacteria
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