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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.59 - glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) and Organism(s) Bacillus subtilis and UniProt Accession O34425

for references in articles please use BRENDA:EC1.2.1.59
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: O34425
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: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
gapdh, glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, chloroplast glyceraldehyde-3-phosphate dehydrogenase, nadp-dependent glyceraldehyde-3-phosphate dehydrogenase, gapdh2, phosphorylating glyceraldehyde-3-phosphate dehydrogenase, gbs gapdh, nadp-dependent glyceraldehydephosphate dehydrogenase, nadp-dependent glyceraldehyde 3-phosphate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
Dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide (phosphate))
-
-
-
-
GAPDH
-
-
-
-
GAPDH2
-
-
-
-
Glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
-
-
-
-
NAD(NADP)-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NAD(P)-dependent G3P dehydrogenase
-
-
-
-
NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
Triosephosphate dehydrogenase (NAD(P))
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating)
NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
CAS REGISTRY NUMBER
COMMENTARY hide
39369-25-0
-
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 + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
show the reaction diagram
-
-
-
?
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
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in phosphoglucose isomerase-disrupted Escherichia coli (KS002) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, S.; Lee, C.H.; Nam, S.W.; Kim, P.
Alteration of reducing powers in an isogenic phosphoglucose isomerase (pgi)-disrupted Escherichia coli expressing NAD(P)-dependent malic enzymes and NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
Lett. Appl. Microbiol.
52
433-440
2011
Bacillus subtilis (O34425), Bacillus subtilis, Bacillus subtilis 168 (O34425)
Manually annotated by BRENDA team