Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.13 - glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) and Organism(s) Saccharolobus solfataricus and UniProt Accession P39460

for references in articles please use BRENDA:EC1.2.1.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharolobus solfataricus
UNIPROT: P39460 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
glyceraldehyde-3-p dehydrogenase, nadp-glyceraldehyde-3-phosphate dehydrogenase, gapa1, nadp-gapdh, gapa-1, glyceraldehyde-3-dehydrogenase, nadp-gpd, photosynthetic gapdh, ov-gapdh, glyceraldehyde-p dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glyceraldehyde-3-phosphate dehydrogenase
-
dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate phosphorylating)
-
-
-
-
GAPDH
-
-
-
-
glyceraldehyde 3-phosphate dehydrogenase (NADP)
-
-
-
-
glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate phosphorylating)
-
-
-
-
glyceraldehyde-P dehydrogenase
-
-
-
-
NAD(P)-GAPDH
-
-
-
-
NADP+-dependent G-3-P dehydrogenase
-
-
-
-
NADP-dependent glyceraldehyde phosphate dehydrogenase
-
-
-
-
NADP-dependent glyceraldehydephosphate dehydrogenase
-
-
-
-
NADP-glyceraldehyde phosphate dehydrogenase
-
-
-
-
NADP-glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NADP-GPD
-
-
-
-
NADP-triose phosphate dehydrogenase
-
-
-
-
NADPH-D-GA3P
-
-
-
-
triosephosphate dehydrogenase (NADP+)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37250-87-6
-
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 + H+
show the reaction diagram
Vmax/Km for NADP+ is 33fold higher compared to Vmax/Km for NAD+
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
Vmax/Km for NADP+ is 33fold higher compared to Vmax/Km for NAD+
NADP+
NAD+
-
activity with NADP+ is about 50fold higher than that determined for NAD+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00041
3-phospho-D-glyceroyl phosphate
pH 6.5, 70°C
0.838
D-glyceraldehyde 3-phosphate
pH 6.5, 70°C
2.2
NAD+
pH 7.5, 50°C
0.067 - 0.271
NADP+
0.074
NADPH
pH 6.5, 70°C
409
phosphate
pH 6.5, 70°C
0.02 - 0.1
NADP+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
both directions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
gluconeogenic pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
148300
sedimentation analysis
37581
4 * 37581, calculated from sequence
37596
x * 37596, calculated from sequence
37611
4 * 37611, laser desorption mass spectrophotometry
39500
155000
-
gel filtration
41000
-
4 * 41000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
tetramer
-
4 * 41000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from ammonium sulfate to produce crystals that diffract to 2.4 A with a space group of P4(3)2(1)2 or P4(1)2(1)2
determination of the crystal structure of the apoenzyme by multiple isomorphous replacement at 2.05 A resolution, hanging drop technique. The crystals belong to space group P4(1)2(1)2 or its enantiomorph with cell dimensions a = b = 102.3 A, c = 181.6 A, which contract upon cryocooling at 100 K to a = b = 101.6 A, c = 179.9 A. The asymmetric unit contains two subunits with a molecular mass of 37611 Da
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
40 min, stable
87
-
half-life: 45 min
95
-
30 min, complete inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heat treatment at 80°C is an effective first step in the purification of these recombinant enzymes from extracts of the Escherichia coli host
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli. The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from Sulfolobus solfataricus overlap by 8-bp
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Russo, A.D.; Rullo, R.; Masullo, M.; Ianniciello, G.; Arcari, P.; Bocchini, V.
Glyceraldehyde 3-phosphate dehydrogenase in the hyperthermophilic archaeon Sulfolobus solfataricus: characterization and significance in glucose metabolism
Biochem. Mol. Biol. Int.
36
123-135
1995
Saccharolobus solfataricus
Manually annotated by BRENDA team
Arcari, P.; Russo, A.; Ianniciello, G.; Gallo, M.; Bocchini, V.
Nucleotide sequence and molecular evolution of the gene coding for glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic archaebacterium Sulfolobus solfataricus
Biochem. Genet.
31
241-252
1993
Saccharolobus solfataricus (P39460)
Manually annotated by BRENDA team
Jones, C.E.; Fleming, T.M.; Cowan, D.A.; Littlechild, J.A.; Piper, P.W.
The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-bp. Isolation, sequencing of the genes and expression in Escherichia coli
Eur. J. Biochem.
233
800-808
1995
Saccharolobus solfataricus (P39460)
Manually annotated by BRENDA team
Isupov, M.N.; Fleming, T.M.; Dalby, A.R.; Crowhurst, G.S.; Bourne, P.C.; Littlechild, J.A.
Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Mol. Biol.
291
651-660
1999
Saccharolobus solfataricus (P39460)
Manually annotated by BRENDA team
Fleming, T.M.; Jones, C.E.; Piper, P.W.; Cowan, D.A.; Isupov, M.N.; Littlechild, J.A.
Characterization, crystallization and preliminary X-ray investigation of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus
Acta Crystallogr. Sect. D
54
671-674
1998
Saccharolobus solfataricus (P39460)
Manually annotated by BRENDA team
Kouril, T.; Esser, D.; Kort J.; Westerhoff, H.V.; Siebers, B.; Snoep, J.L.
Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted system of gluconeogenesis in Sulfolobus solfataricus
FEBS J.
280
4666-4680
2013
Saccharolobus solfataricus (P39460), Saccharolobus solfataricus P2 (P39460)
Manually annotated by BRENDA team