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Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Caenorhabditis elegans

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IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
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This record set is specific for:
Caenorhabditis elegans
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoglyceraldehyde dehydrogenase
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-
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BARS-38
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CP 17/CP 18
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dehydrogenase, glyceraldehyde phosphate
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-
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dihydrogenase, glyceraldehyde phosphate
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-
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G3PD
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-
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GAPDH
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-
-
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GAPDH1
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-
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GAPDH2
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-
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glyceraldehyde phosphate dehydrogenase (NAD)
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-
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glyceraldehyde-3-P-dehydrogenase
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-
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glyceraldehyde-3-phosphate dehydrogenase (NAD)
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-
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GPD
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-
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Gra3PDH
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-
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GraP-DH
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-
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Larval antigen OVB95
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-
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Major larval surface antigen
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-
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NAD+-G-3-P dehydrogenase
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NAD-dependent glyceraldehyde phosphate dehydrogenase
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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
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NAD-G3PDH
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-
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NADH-glyceraldehyde phosphate dehydrogenase
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-
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P-37
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phosphoglyceraldehyde dehydrogenase
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Plasmin receptor
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Plasminogen-binding protein
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-
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TLAb
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triose phosphate dehydrogenase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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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 hide
9001-50-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
additional information
?
-
-
activity of isoenzyme 2 increases during postembryonic development
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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activity of isoenzyme 2 increases during postembryonic development
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isoenzyme 2 is body-wall muscle specific activity located within the actin-containing I and A zones of the nematode‘s sarcomers
Manually annotated by BRENDA team
additional information
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isoenzyme 1 is present in all cells
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G3P2_CAEEL
341
0
36455
Swiss-Prot
Mitochondrion (Reliability: 4)
G3P3_CAEEL
341
0
36459
Swiss-Prot
Mitochondrion (Reliability: 4)
G3P4_CAEEL
341
0
36427
Swiss-Prot
Mitochondrion (Reliability: 4)
G3P1_CAEEL
341
0
36382
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
131000
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gel filtration
38500
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4 * 38500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 38500, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoenzyme 1 and 2
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of complete nucleotide sequence of the coding as well as the noncoding flanking regions of the gene
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yarbrough, P.O.; Hayden, M.A.; Dunn, L.A.; Vermersch, P.S.; Klass, M.R.; Hecht, R.M.
The glyceraldehyde-3-phosphate dehydrogenase gene family in the nematode, Caenorhabditis elegans: isolation and characterization of one of the genes
Biochim. Biophys. Acta
908
21-33
1987
Caenorhabditis elegans
Manually annotated by BRENDA team
Yarbrough, P-O.; Hecht, R.M.
Two isoenzymes of glyceraldehyde-3-phosphate dehydrogenase in Caenorhabditis elegans. Isolation, properties, and immunochemical characterization
J. Biol. Chem.
259
14711-14720
1984
Caenorhabditis elegans
Manually annotated by BRENDA team