Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) Contents Function Nomenclature References Further reading Navigation menu1.2.1.1337250-87-6 IntEnz viewBRENDA entryNiceZyme viewKEGG entrymetabolic pathwayprofileRCSB PDBPDBePDBsumAmiGO QuickGOarticlesarticlesproteins1.2.1.131380419010.1016/0076-6879(55)01067-713271400eeexpanding ite
Aldehyde dehydrogenaseAcetaldehyde dehydrogenaseLong-chain-aldehyde dehydrogenaseAldehyde oxidasePyruvate synthaseActive siteBinding siteCatalytic triadOxyanion holeEnzyme promiscuityCatalytically perfect enzymeCoenzymeCofactorEnzyme catalysisEC numberEnzyme superfamilyEnzyme familyList of enzymesOxidoreductaseslistTransferaseslistHydrolaseslistLyaseslistIsomeraseslistLigaseslistTranslocaseslist
EC 1.2.1NADPH-dependent enzymesEnzymes of known structure
enzymologyEC1.2.1.13enzymecatalyzeschemical reactionsubstratesD-glyceraldehyde 3-phosphatephosphateNADP+products3-phospho-D-glyceroyl phosphateNADPHH+oxidoreductasesCalvin cycleautotrophiccarbon fixationsystematic name
glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) | |||||||||
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Identifiers | |||||||||
EC number | 1.2.1.13 | ||||||||
CAS number | 37250-87-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) (EC 1.2.1.13) is an enzyme that catalyzes the chemical reaction
- D-glyceraldehyde 3-phosphate + phosphate + NADP+⇌displaystyle rightleftharpoons 3-phospho-D-glyceroyl phosphate + NADPH + H+
The 3 substrates of this enzyme are D-glyceraldehyde 3-phosphate, phosphate, and NADP+, whereas its 3 products are 3-phospho-D-glyceroyl phosphate, NADPH, and H+.
Contents
1 Function
2 Nomenclature
3 References
4 Further reading
Function
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in the Calvin cycle which is an autotrophic carbon fixation pathway.
Nomenclature
The systematic name of this enzyme class is D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating). Other names in common use include:
- dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating)
- GAPDH
- glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphorylating)
- glyceraldehyde-3-phosphate dehydrogenase (NADP) (phosphorylating)
- NADP-dependent glyceraldehyde phosphate dehydrogenase
- NADP-glyceraldehyde phosphate dehydrogenase
- NADP-glyceraldehyde-3-phosphate dehydrogenase
- NADP-triose phosphate dehydrogenase
- triosephosphate dehydrogenase (NADP)
References
Further reading
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Brenneman FN, Volk WA (1959). "Glyceraldehyde phosphate dehydrogenase activity with triphosphopyridine nucleotide and with diphosphopyridine nucleotide". J. Biol. Chem. 234: 2443–7. PMID 13804190..mw-parser-output cite.citationfont-style:inherit.mw-parser-output .citation qquotes:"""""""'""'".mw-parser-output .citation .cs1-lock-free abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-subscription abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registrationcolor:#555.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration spanborder-bottom:1px dotted;cursor:help.mw-parser-output .cs1-ws-icon abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center.mw-parser-output code.cs1-codecolor:inherit;background:inherit;border:inherit;padding:inherit.mw-parser-output .cs1-hidden-errordisplay:none;font-size:100%.mw-parser-output .cs1-visible-errorfont-size:100%.mw-parser-output .cs1-maintdisplay:none;color:#33aa33;margin-left:0.3em.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-formatfont-size:95%.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-leftpadding-left:0.2em.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-rightpadding-right:0.2em
Gibbs M (1955). "TPN triosephosphate dehydrogenase from plant tissue". Methods Enzymol. 1: 411–415. doi:10.1016/0076-6879(55)01067-7.
Rosenberg LL, Arnon DI (1955). "The preparation and properties of a new glyceraldehyde-3-phosphate dehydrogenase from photosynthetic tissues". J. Biol. Chem. 217 (1): 361–71. PMID 13271400.
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EC 1.2.1, Enzymes of known structure, NADPH-dependent enzymesUncategorized