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Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Mus musculus
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1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
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Word Map
- 1.2.1.12
- tetramer
- chloroplast
-
gapcs
- streptococcal
- stearothermophilus
- glomerulonephritis
-
nadp-dependent
-
genorm
-
normfinder
- medicine
- 3-phosphoglycerate
-
phosphofructokinase
- flagellum
-
poststreptococcal
- 1,3-bisphosphoglycerate
-
bestkeeper
- lobster
- glycosomal
-
2.7.1.11
-
glyceraldehyde-phosphate
-
nephritogenic
-
4.1.2.13
- plr
-
2.7.2.3
-
endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
gapdhs, d-glyceraldehyde-3-phosphate dehydrogenase, gapds, gadph, glyceraldehyde-3-phosphate dehydrogenases, plasmin receptor, gapc1, plasminogen-binding protein, gapcp, glyceraldehyde-3 phosphate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-phosphoglyceraldehyde dehydrogenase
-
-
-
-
BARS-38
-
-
-
-
CP 17/CP 18
-
-
-
-
D-glyceraldehyde-3-phosphate dehydrogenase
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
-
-
-
-
GAPDH
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-dehydrogenase
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NAD)
-
-
-
-
GPD
-
-
-
-
Gra3PDH
-
-
-
-
GraP-DH
-
-
-
-
Larval antigen OVB95
-
-
-
-
Major larval surface antigen
-
-
-
-
NAD+-G-3-P dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde phosphate dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NAD-G3PDH
-
-
-
-
NADH-glyceraldehyde phosphate dehydrogenase
-
-
-
-
P-37
-
-
-
-
phosphoglyceraldehyde dehydrogenase
-
-
-
-
Plasmin receptor
-
-
-
-
Plasminogen-binding protein
-
-
-
-
TLAb
-
-
-
-
triose phosphate dehydrogenase
-
-
-
-
GAPDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
CAS REGISTRY NUMBER
COMMENTARY
9001-50-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
additional information
?
-
-
GAPDH is a Ca2+-dependent substrate of phosphorylase kinase although the rate of phosphorylation is very slow
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-morpholino-sydnonimine
-
the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme. The superoxide anion released by 3-morpholino-sydnonimine potentiates the inactivation
pseudo-GAPDH
psiGAPDH peptide, an inhibitor of psiPKC-mediated GAPDH phosphorylation that does not inhibit the phosphorylation of other deltaPKC substrates. psiGAPDH peptide is also an inhibitor of GAPDH oligomerization and thus an inhibitor of GAPDH glycolytic activity. psiGAPDH peptide treatment causes damage in an ex vivo model of myocardial infarction
-
sodium nitroprusside
-
the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme
T0501_7749
2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, a small-molecule, highly selective isozyme GAPDHS inhibitor, molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview; 2-[2-amino-3-(4-methylphenyl)sulfonylpyrrolo[3,2-b]quinoxalin-1-yl]-1-(4-nitrophenyl)ethanol, a small-molecule, highly selective isozymeGAPDHS inhibitor, the compound causes significant reductions in mouse sperm lactate production and in the percentage of motile mouse sperm. Molecular docking simulations in GAPDHS and GAPDH isozymes, binding structure, overview
T0506_9350
1-cyclohexyl-3-[4-[(4-methoxyphenyl)sulfamoyl]-2-nitroanilino]urea, a partial selective isozyme GAPDH inhibitor, binding structure, overview. T0506_9350 inhibition of human and mouse tGAPDHS is competitive with both D-glyceraldehyde 3-phosphate and NAD+
Trinitrobenzenesulfonic acid
-
inactivation with pseudo-first-order kinetics. D-glyceraldehyde-3-phosphate, NAD+, NADH and 3-phospho-D-glyceroyl phosphate almost completely protect from inactivation
additional information
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo. Oxidative stress inhibits the protective GAPDH-mediated elimination of damaged mitochondria. Rational design of a peptide based on homology between deltaPKC and GAPDH
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0569
T0506_9350
versus NAD+, pH and temperature not specified in the publication
0.071
T0506_9350
versus D-glyceraldehyde 3-phosphate, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
epididymal spermatozoa, localization of the GAPDHS protein in the sperm head, immunologic analysis, in the principal piece and acrosomal part of the sperm cells, overview
sperm-specific glyceraldehyde 3-phosphate dehydrogenase, restricted enzyme expression during spermatogenesis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the localization of enzyme mutant 4K-R-GAPDH remains primarily perinuclear in the basal state, similar to wild-type enzyme GAPDH in cells
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
FAO hepatoma cells with mutations of all 4 lysine residues (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state show reduced GAPDH glycolytic activity and glycolytic flux and increased gluconeogenic GAPDH activity and glucose production. Hepatic expression of mutant 4K-R-GAPDH in mice increases GAPDH gluconeogenic activity and the contribution of gluconeogenesis to endogenous glucose production in the unfed state. Consistent with the increased reliance on the energy-consuming gluconeogenic pathway, plasma free fatty acids and ketones are elevated inmice expressing 4K-RGAPDH, suggesting enhanced lipolysis and hepatic fatty acid oxidation. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice
malfunction
GAPDHS inhibitor effects on sperm motility and metabolism, overview
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that catalyzes the conversion of glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has a non-catalytic (thus a noncanonical) role in inducing mitochondrial elimination under oxidative stress. Phosphorylation of GAPDH by delta protein kinase C (deltaPKC) inhibits the GAPDH-dependent mitochondrial elimination. deltaPKC phosphorylation of GAPDH correlates with increased cell injury following oxidative stress, suggesting that inhibiting GAPDH phosphorylation decreases cell injury
physiological function
glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, GAPDHS, is a sperm-specific glycolytic enzyme involved in energy production during spermatogenesis and sperm motility
physiological function
-
reversible post-translational modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), particularly acetylation, contributes to the reciprocal regulation of glycolysis/gluconeogenesis. Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
additional information
-
detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme of mouse and human, homology modeling of human and mouse GAPDH and GAPDHS isozymes, and binding sites for GAP and NAD+, determined by reference to structures PDB 1DC4 and 1DC6 and crystal structure of Palinurus versicolor GAPDH, PDB ID 1CRW, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G3PT_MOUSE
440
0
47657
Swiss-Prot
Mitochondrion (Reliability: 5)
G3P_MOUSE
333
0
35810
Swiss-Prot
Mitochondrion (Reliability: 3)
S4R257_MOUSE
280
0
29939
TrEMBL
other Location (Reliability: 1)
A0A0R4J0X7_MOUSE
438
0
47443
TrEMBL
Mitochondrion (Reliability: 5)
A0A0A0MQF6_MOUSE
359
0
38653
TrEMBL
Mitochondrion (Reliability: 3)
S4R1W1_MOUSE
333
0
35812
TrEMBL
Mitochondrion (Reliability: 3)
A0A1D5RLD8_MOUSE
333
0
35812
TrEMBL
Mitochondrion (Reliability: 3)
D2KHZ9_MOUSE
333
0
35810
TrEMBL
Mitochondrion (Reliability: 3)
S4R2G5_MOUSE
440
0
47643
TrEMBL
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
either treatment with psiGAPDH or direct phosphorylation of GAPDH by deltaPKC decreased GAPDH tetramerization, which corresponded to reduced GAPDH glycolytic activity in vitro and ex vivo
?
x * 75000, about, recombinant enzyme, SDS-PAGE, x * 45000-50000, native enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylation
-
acetylation of lysine residues Lys115, -160, -225, and -252 as post-translational modification of glyceraldehyde-3-phosphate dehydrogenase. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice. Lys115, -225, and -252 are acetylated in a coordinated manner by the p300/cAMP response element-binding protein (CBP)-associated factor acetyltransferase, whereas Lys160 is acetylated by the p300/CBP acetyltransferase
phosphoprotein
phosphorylation of GAPDH by delta protein kinase C (deltaPKC). When deltaPKC is inactive, its GAPDH-docking site may be occupied by a pseudo-GAPDH (psiGAPDH) site, a GAPDH-like sequence that mimics the deltaPKC-binding site on GAPDH, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant apo-enzyme tGAPDHS, hanging-drop vapor-diffusion method, 3 mg/ml protein in PBS is mixed in a 1:1 volume ratio with reservoir solution containing 0.2 M potassium thiocyanate, 0.1 M Bis-Tris propane, pH 6.5, and 20% PEG 3350, 20°C, 6 days, X-ray diffraction structure determination and analysis at 2.01 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A229V
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
C281W
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
G166D
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
I308S
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
V239I
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
Y327N
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
additional information
additional information
-
mutants Gapdhm1Neu (Y91stop truncated protein of 89 amino acids), Gapdhm2Neu (truncated/altered protein of 9 amino acids), and Gapdhm8Neu (truncated/altered protein of 73 amino acids) exhibit 50-55% residual activity in blood compared to the wild type enzyme
additional information
-
generation of FAO hepatoma cells with mutations of all 4 lysine residues K115, K160, K225, and K252 (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state reduces GAPDH glycolytic activity and glycolytic flux and increases gluconeogenic GAPDH activity and glucose production, phenotype overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged GAPDH from gapA-deficient Escherichia coli strain DS112 by glutathione affinity chromatography, and on-column cleavage of the GST-tag by bovine thrombin before elution of the enzyme
recombinant MBP-tagged tGAPDHS from gapA-deficient Escherichia coli strain DS112 by amylose affinity chromatography, followed by cleavage of the MBP-tag by bovine thrombin dialysis, and anion exchange chromatography
use of glyceraldehyde-3-phosphate dehydrogenase-depleted human erythrocyte ghosts as specific high affinity adsorbents for the purification
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expression of GST-tagged GAPDH in gapA-deficient Escherichia coli strain DS112
recombinant enzyme expression of MBP-tagged tGAPDHS (amino acids 106-438) in gapA-deficient Escherichia coli strain DS112
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
in experimental autoimmune encephalomyelitis, the proportion of S-nitrosylated neurofilament proteins, NMDA receptors, alpha/beta-tubulin, beta-actin, and GAPDH is increased. Neuronal specific enolase is the major S-nitrosylated protein in acute experimental autoimmune encephalomyelitis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ghosh, S.; Mukherjee, K.; Ray, M.; Ray, S.
Identification of a critical lysine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cell. Comparison with the rabbit muscle enzyme
Eur. J. Biochem.
268
6037-6044
2001
Oryctolagus cuniculus, Mus musculus
Saleemuddin, M.; Zimmermann, U.
Use of glyceraldehyde-3-phosphate dehydrogenase-depleted human erythrocyte ghosts as specific high affinity adsorbents for the purification of glyceraldehyde-3-phosphate dehydrogenase from various tissues
Biochim. Biophys. Acta
527
182-192
1978
Mus musculus
Marin, P.; Maus, M.; Bockaert, J.; Glowinski, J.; Premont, J.
Oxygen free radicals enhance the nitric oxide-induced covalent NAD(+)-linkage to neuronal glyceraldehyde-3-phosphate dehydrogenase
Biochem. J.
309
891-898
1995
Mus musculus
Boulatnikov, I.G.; Nadeau, O.W.; Daniels, P.J.; Sage, J.M.; Jeyasingham, M.D.; Villar, M.T.; Artigues, A.; Carlson, G.M.
The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase
Biochemistry
47
7228-7236
2008
Mus musculus
Kuravsky, M.L.; Muronetz, V.I.
Somatic and sperm-specific isoenzymes of glyceraldehyde-3-phosphate dehydrogenase: comparative analysis of primary structures and functional features
Biochemistry
72
744-749
2007
Bos taurus, Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus
Shalova, I.N.; Cechalova, K.; Rehakova, Z.; Dimitrova, P.; Ognibene, E.; Caprioli, A.; Schmalhausen, E.V.; Muronetz, V.I.; Saso, L.
Decrease of dehydrogenase activity of cerebral glyceraldehyde-3-phosphate dehydrogenase in different animal models of Alzheimers disease
Biochim. Biophys. Acta
1770
826-832
2007
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus
Pretsch, W.; Favor, J.
Genetic, biochemical, and molecular characterization of nine glyceraldehyde-3-phosphate dehydrogenase mutants with reduced enzyme activity in Mus musculus
Mamm. Genome
18
686-692
2007
Mus musculus
Bizzozero, O.A.; Zheng, J.
Identification of major S-nitrosylated proteins in murine experimental autoimmune encephalomyelitis
J. Neurosci. Res.
87
2881-2889
2009
Mus musculus
Bond, S.T.; Howlett, K.F.; Kowalski, G.M.; Mason, S.; Connor, T.; Cooper, A.; Streltsov, V.; Bruce, C.R.; Walder, K.R.; McGee, S.L.
Lysine post-translational modification of glyceraldehyde-3-phosphate dehydrogenase regulates hepatic and systemic metabolism
FASEB J.
31
2592-2602
2017
Mus musculus, Mus musculus C57BL6
Qvit, N.; Joshi, A.U.; Cunningham, A.D.; Ferreira, J.C.; Mochly-Rosen, D.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein-protein interaction inhibitor reveals a non-catalytic role for GAPDH oligomerization in cell death
J. Biol. Chem.
291
13608-13621
2016
Anolis carolinensis (H9GBL1), Gallus gallus (P00356), Homo sapiens (P04406), Rattus norvegicus (P04797), Mus musculus (P16858), Danio rerio (Q6NYI5), Rattus norvegicus Wistar (P04797)
Danshina, P.; Qu, W.; Temple, B.; Rojas, R.; Miley, M.; Machius, M.; Betts, L.; OBrien, D.
Structural analyses to identify selective inhibitors of glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme
Mol. Hum. Reprod.
22
410-426
2016
Homo sapiens (O14556), Homo sapiens (P04406), Homo sapiens, Mus musculus (P16858), Mus musculus (Q64467), Mus musculus
Margaryan, H.; Dorosh, A.; Capkova, J.; Manaskova-Postlerova, P.; Philimonenko, A.; Hozak, P.; Peknicova, J.
Characterization and possible function of glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS in mammalian sperm
Reprod. Biol. Endocrinol.
13
15
2015
Homo sapiens (O14556), Homo sapiens, Mus musculus (Q64467), Mus musculus, Mus musculus BALB/c (Q64467)
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