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Information on EC 1.1.1.94 - glycerol-3-phosphate dehydrogenase [NAD(P)+] and Organism(s) Rickettsia prowazekii and UniProt Accession Q9ZDA0

for references in articles please use BRENDA:EC1.1.1.94
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IUBMB Comments
The enzyme from Escherichia coli shows specificity for the B side of NADPH.
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This record set is specific for:
Rickettsia prowazekii
UNIPROT: Q9ZDA0
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Word Map
The taxonomic range for the selected organisms is: Rickettsia prowazekii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
sn-glycerol-3-phosphate dehydrogenase, cvgpd1, nadp-dependent glycerol-3-phosphate dehydrogenase, nad(p)h-dependent glycerol-3-phosphate dehydrogenase, rp442, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycerol 3-phosphate dehydrogenase (NADP)
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glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate))
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L-glycerol-3-phosphate:NAD(P) oxidoreductase
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NAD(P)H-dependent dihydroxyacetone-phosphate reductase
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NAD(P)H-dependent glycerol-3-phosphate dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase
The enzyme from Escherichia coli shows specificity for the B side of NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-30-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerone phosphate + NADH + H+
sn-glycerol 3-phosphate + NAD+
show the reaction diagram
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r
glycerone phosphate + NADPH + H+
sn-glycerol 3-phosphate + NADP+
show the reaction diagram
favoured reaction direction
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r
sn-glycerol 3-phosphate + NADP+
glycerone phosphate + NADPH + H+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
NADPH is preferred over NADH as the cofactor
NADPH
NADPH is preferred over NADH as the cofactor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.528
glycerone phosphate
cosubstrate NADPH, pH 7.4, temperature not specified in the publication
0.048
NADPH
pH 7.4, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Rickettsia prowazekii is unable to synthesize glycerone phosphate as a substrate for the GpsA enzymatic reaction. Purified Rickettsia prowazekii transports and incorporates glycerone phosphate into phospholipids, implicating a role for GpsA in vivo as part of a rickettsial G3P acquisition pathway for phospholipid biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36600
x * 36600, SDS-PAGE and calculated for His-tagged protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 36600, SDS-PAGE and calculated for His-tagged protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Frohlich, K.M.; Roberts, R.A.; Housley, N.A.; Audia, J.P.
Rickettsia prowazekii uses an sn-glycerol-3-phosphate dehydrogenase and a novel dihydroxyacetone phosphate transport system to supply triose phosphate for phospholipid biosynthesis
J. Bacteriol.
192
4281-4288
2010
Rickettsia prowazekii (Q9ZDA0), Rickettsia prowazekii
Manually annotated by BRENDA team