Any feedback?
Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Bos taurus
for references in articles please use BRENDA:EC1.2.1.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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: Bos taurus
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
-
-
-
-
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
-
-
-
-
GAPDH
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-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
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
additional information
?
-
-
the enzyme is a GABA(A) receptor kinase linking glycolysis to neuronal inhibition
-
-
?
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
-
-
-
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+
-
-
-
?
additional information
?
-
-
the enzyme is a GABA(A) receptor kinase linking glycolysis to neuronal inhibition
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
differing occupancy by NAD, bGAPDH(NAD)4, and bGAPDH(NAD)3 in the homotetramer, structure analysis, overview. Importance of Phe34 in NAD+ binding, Phe34 is stabilized in the presence of NAD+ but displays greater mobility in its absence. The oxidative state of the active site Cys149 residue is regulated by NAD+ binding, because this residue is found oxidized in the absence of dinucleotide. The distance between Cys149 and His176 decreases upon NAD binding and Cys149 remains in a reduced state when NAD+ is bound. Dual side-chain conformations are observed in Ser207 in subunits of O, Q, and R of the bGAPDH(NAD)3. Residues Pro33 and Phe34 form a bottleneck for NAD+ binding
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
10 mM, 2fold activation of the oxidation of D-glyceraldehyde 3-phosphate
dithioerythritol
-
10 mM, 2fold activation of the oxidation of D-glyceraldehyde 3-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.153
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
7.8 - 8.1
-
oxidation of D-glyceraldehyde 3-phosphate, Tris buffer and triethanolamine buffer
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme reversibly interacts with a protease-sensitive plasma membrane-specific protein of rad outer segments
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
substitution of Phe34 with smaller side chain (e.g. Gly or Leu), or polar residue (e.g. Thr) abolishes the NAD+ binding affinity, or reduce the protein's catalytic efficiency
physiological function
the enzyme plays a central role in glycolysis, and nonglycolytic processes such as nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis
additional information
importance of Phe34 in NAD+ binding, Phe34 is stabilized in the presence of NAD+ but displays greater mobility in its absence. The oxidative state of the active site Cys149 residue is regulated by NAD+ binding, because this residue is found oxidized in the absence of dinucleotide. The distance between Cys149 and His176 decreases upon NAD binding and Cys149 remains in a reduced state when NAD+ is bound, cofactor binding and active site structures, catalytic mechanism, 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). G3P_BOVIN
333
0
35868
Swiss-Prot
Mitochondrion (Reliability: 3)
G3PT_BOVIN
395
0
43288
Swiss-Prot
other Location (Reliability: 4)
Q712W6_BOVIN
268
0
28755
TrEMBL
other Location (Reliability: 5)
A0A3Q1M8J9_BOVIN
376
0
40520
TrEMBL
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
structure analysis, overview. Dual side-chain conformations are observed in Ser207 in subunits of O, Q, and R of the bGAPDH(NAD)3
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified native tetrameric enzyme with either three or four bound NAD+ molecules, bGAPDH can be crystallized directly from isotonic extracts of ROS, X-ray diffraction structure determination and analysis at 1.93 A and 1.54 A resolution, respectively, molecular replacement using the coordinates of one monomer of rabbit-muscle GAPDH, PDB ID 1J0X, without ligand and water to search the initial model, modelling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from bovine retinas using NAD+-agarose affinity chromatography
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hsu, S.C.; Molday, R.S.
Glyceraldehyde-3-phosphate dehydrogenase is a major protein associated with the plasma membrane of retinal photoreceptor outer segments
J. Biol. Chem.
265
13308-13313
1990
Bos taurus
Kocha, T.; Fukuda, T.; Isobe, T.; Okuyama, T.
Specific purification of glyceraldehyde-3-phosphate dehydrogenase by hydrophobic chromatography on immobilized colchicine
Biochim. Biophys. Acta
991
56-61
1989
Bos taurus
Harris, J.I.; Waters, M.
Glyceraldehyde-3-phosphate dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
1-49
1976
Geobacillus stearothermophilus, Bacillus cereus, Bos taurus, Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Felis catus, Hippoglossus sp., Homo sapiens, Lobster, Meleagris gallopavo, Pisum sativum, Rattus norvegicus, Acipenser sp., Sus scrofa, Thermus aquaticus
-
Heinz, F.; Kulbe, K.D.
Glyceraldehydephosphate dehydrogenase from liver. I. Isolation and characterization of the bovine liver enzyme
Hoppe-Seyler's Z. Physiol. Chem.
351
249-262
1970
Bos taurus
Laschet, J.J.; Minier, F.; Kurcewicz, I.; Bureau, M.H.; Trottier, S.; Jeanneteau, F.; Griffon, N.; Samyn, B.; Van Beeumen, J.; Louvel, J.; Sokoloff, P.; Pumain, R.
Glyceraldehyde-3-phosphate dehydrogenase is a GABAA receptor kinase linking glycolysis to neuronal inhibition
J. Neurosci.
24
7614-7622
2004
Bos taurus
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
EXTERNAL LINKS (specific for EC-Number 1.2.1.12)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
