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)
Identifiers
EC number1.2.1.13
CAS number37250-87-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile

PDB structures		RCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO






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.








EC 1.2.1, Enzymes of known structure, NADPH-dependent enzymesUncategorized
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