KEGG   ENZYME: 1.2.1.90Help
Entry
EC 1.2.1.90                 Enzyme                                 

Name
glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+];
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase;
GAPN
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
D-glyceraldehyde-3-phosphate:NAD(P)+ oxidoreductase
Reaction(IUBMB)
D-glyceraldehyde 3-phosphate + NAD(P)+ + H2O = 3-phospho-D-glycerate + NAD(P)H + 2 H+ [RN:R01058 R10860]
Reaction(KEGG)
Substrate
D-glyceraldehyde 3-phosphate [CPD:C00118];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Product
3-phospho-D-glycerate [CPD:C00197];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)].
History
EC 1.2.1.90 created 2014
Pathway
ec00010  Glycolysis / Gluconeogenesis
ec00030  Pentose phosphate pathway
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K18978  glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]
Genes
TACI: TDSAC_0307
PFU: PF0755
PFI: PFC_02935
TKO: TK0705
TSI: TSIB_1868
TLT: OCC_12546
TNU: BD01_0877
THV: ADU37_CDS19860
TCE: A3L02_05455
TTD: A3L14_07265
PPAC: PAP_03390
HAL: VNG_0937G(gap)
HSL: OE_2367F(aldH3)
HHB: Hhub_2122
NMO: Nmlp_1397(aldH2)
HTU: Htur_1629
NMG: Nmag_3488
NAT: NJ7G_3347
APE: APE_1786.1(gapN)
ACJ: ACAM_1119(gapN)
SMR: Smar_0084
DKA: DKAM_1444
TAG: Tagg_1262
IAG: Igag_1780
STO: STK_24770(gapN)
SSO: SSO3194(gapN-3)
SOL: Ssol_0932
SSOA: SULA_0965
SSOL: SULB_0967
SSOF: SULC_0966
SAI: Saci_0227
SID: M164_2168
SII: LD85_2431
SIH: SiH_2110
SIR: SiRe_2042
SIC: SiL_2017
MSE: Msed_1298
MCN: Mcup_0943
PAS: Pars_0554
POG: Pogu_1837
CMA: Cmaq_0979
TUZ: TUZN_1133
TTN: TTX_1169(gapN)
VDI: Vdis_2334
VMO: VMUT_0605
ASC: ASAC_1423
NAA: Nps_02395
 » show all
Taxonomy
Reference
1  [PMID:9497334]
  Authors
Brunner NA, Brinkmann H, Siebers B, Hensel R
  Title
NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties.
  Journal
J Biol Chem 273:6149-56 (1998)
DOI:10.1074/jbc.273.11.6149
  Sequence
Reference
2  [PMID:11354453]
  Authors
Brunner NA, Siebers B, Hensel R
  Title
Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation  on protein and transcript level.
  Journal
Extremophiles 5:101-9 (2001)
  Sequence
Reference
3  [PMID:11842090]
  Authors
Pohl E, Brunner N, Wilmanns M, Hensel R
  Title
The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
  Journal
J Biol Chem 277:19938-45 (2002)
DOI:10.1074/jbc.M112244200
  Sequence
Reference
4  [PMID:15288789]
  Authors
Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E
  Title
Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax.
  Journal
J Mol Biol 341:815-28 (2004)
DOI:10.1016/j.jmb.2004.05.032
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.90
IUBMB Enzyme Nomenclature: 1.2.1.90
ExPASy - ENZYME nomenclature database: 1.2.1.90
BRENDA, the Enzyme Database: 1.2.1.90

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