Information on EC 1.1.1.261 - sn-glycerol-1-phosphate dehydrogenase

for references in articles please use BRENDA:EC1.1.1.261
Word Map on EC 1.1.1.261
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.261
-
RECOMMENDED NAME
GeneOntology No.
sn-glycerol-1-phosphate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CDP-archaeol biosynthesis
-
-
lipid metabolism
-
-
Glycerophospholipid metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase
This enzyme is found primarily as a Zn2+-dependent form in Archaea but a Ni2+-dependent form has been found in Gram-positive bacteria [6]. The Zn2+-dependent metalloenzyme is responsible for the formation of Archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in Archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol synthase) to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [4]. Activity of the enzyme is stimulated by K+ [2].
CAS REGISTRY NUMBER
COMMENTARY hide
204594-18-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Commonote archaea
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
Commonote archaea
-
reconstruction of molecular phylogenetic trees of glycerol-1-phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase and glycerol kinase. The archaeal common ancestor probably possessed a glycerol-3-phosphate-lipid membrane synthesized enzymatically, after which the archaeal lineage acquired glycerol-1-phosphate dehydrogenase followed by the replacement of a glycerol-3-phosphate-lipid membrane with a glycerol-1-phosphate-lipid membrane
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate + NAD(P)H
sn-glycerol-1-phosphate + NAD(P)+
show the reaction diagram
dihydroxyacetone phosphate + NADH + H+
sn-glycerol 1-phosphate + NAD+
show the reaction diagram
dihydroxyacetone phosphate + NADH + H+
sn-glycerol-1-phosphate + NAD+
show the reaction diagram
dihydroxyacetone phosphate + NADPH + H+
sn-glycerol 1-phosphate + NADP+
show the reaction diagram
dihydroxyacetone phosphate + NADPH + H+
sn-glycerol-1-phosphate + NADP+
show the reaction diagram
dihydroxyacetonephosphate + NAD(P)H
glycerol 1-phosphate + NAD(P)+
show the reaction diagram
dihydroxyacetonephosphate + NAD(P)H
glycerol-1-phosphate + NAD(P)+
show the reaction diagram
sn-glycerol-1-phosphate + NAD+
dihydroxyacetone phosphate + NADH
show the reaction diagram
additional information
?
-
-
no activity with glycerol-2-phosphate, glycerol-3-phosphate, glyceraldehyde phosphate, glycerol, and dihydroxyacetone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dihydroxyacetone phosphate + NAD(P)H
sn-glycerol-1-phosphate + NAD(P)+
show the reaction diagram
dihydroxyacetonephosphate + NAD(P)H
glycerol 1-phosphate + NAD(P)+
show the reaction diagram
dihydroxyacetonephosphate + NAD(P)H
glycerol-1-phosphate + NAD(P)+
show the reaction diagram
-
the enzyme is involved in formation of the enantiomeric glycerophosphate backbone structure of archaeal phospholipids, metabolic pathway possibilities, overview
-
-
r
sn-glycerol-1-phosphate + NAD+
dihydroxyacetone phosphate + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
about 20% of the activity with Zn2+
Co2+
about 150% of the activity with Zn2+
K+
-
maximum activity at 60-80 mM
Mg2+
about 20% of the activity with Zn2+
Mn2+
about 20% of the activity with Zn2+
Na+
-
maximum activity 20-25 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
slight inhibition at 1 mM
Cu2+
-
slight inhibition at 1 mM
DTT
-
45% inhibition at 1 mM
K+
-
slight inhibition at 70 mM
Na+
-
slight inhibition at 70 mM
NAD(P)+
-
competitive with NAD(P)H and noncompetitive with dihydroxyacetone phosphate
Ni2+
-
slight inhibition at 1 mM
sn-glycerol-1-phosphate
-
noncompetitive with dihydroxyacetone phosphate and NAD(P)H
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
an optimum concentration of about 150 mM KCl produces a more than 400% increase in activity compared with an absence of KCl; the optimum concentration of about 150 mM KCl produces more than 400% increase in activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 2.17
dihydroxyacetone phosphate
4.8 - 16.3
glycerol-1-phosphate
0.127 - 1.57
NAD+
0.032 - 0.415
NADH
0.27
NADP+
-
glycerol-1-phosphate oxidation
0.006 - 0.165
NADPH
8.92
sn-glycerol-1-phosphate
-
pH 7.0, 65C
additional information
additional information
-
kinetic analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 60.47
dihydroxyacetone phosphate
0.09
NAD+
-
pH 7.0, 65C
2.4 - 11
NADH
0.044 - 7
NADPH
0.09
sn-glycerol-1-phosphate
-
pH 7.0, 65C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.96 - 14
dihydroxyacetone phosphate
23.67 - 142
NADH
8.71 - 1155
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.22
-
purified enzyme, pH 7.0, 65C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
in MES buffer or MOPS buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 7.7
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
94 - 96
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 85
-
at temperatures higher than 85C no activity of the enzyme can be detected due to precipitation
55 - 96
-
-
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
SDS-PAGE
43000
1 * 43000, SDS-PAGE
72400
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 38000, SDS-PAGE
monomer
octamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 30% (w/v) poly(ethylene glycol) methyl ether 550/polyethylene glycol 20000 and 0.1 M HEPES, pH 7.6; structure with bound substrate dihydroxyacetone phosphate, product glycerol 1-phosphate, NADPH, and Zn2+ cofactor. The sole role of His226, His247, and Asp148 is to coordinate the active site Zn2+. A pro-R hydride transfer/relay system is in operation during catalysis, mediated by water and completed by the polarization of the carbonyl of dihydroxyacetone phosphate by Zn2+. Residue Asn104 may influence affinity for the coenzyme and the rate of reaction via its interaction with NADPH
to 2.45 A resolution, one homohexamer per asymmetric unit, with presence of the bound cofactor NADPH in subunits D, E, and F. The phosphate group at C2' of the adenine ribose of NADPH is tightly held through the five biased hydrogen bonds with Ser40 and Thr42. The NADPH molecule is pushed away from the normal coenzyme binding site
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
decrease of activity below
207960
6.8
-
at pH 6.8 86-91% of activity is detected
668020
7.4
-
decrease of activity above
207960
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51
-
temperature-induced conformational change
90
-
half-life: 2 h
95
-
half-life: 0.5 h
96
-
unstable above 96C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 50 mM Tris-HCl buffer (pH 8.0) containing ZnCl2, 1 h, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography
recombinant protein
to homogeneity, 7step chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli Rosetta 2 (DE3) cells
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
-
expression in Escherichia coli
phylogenetic analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144A
-
lower activity compared to the wild type enzyme
D144N
-
lower activity compared to the wild type enzyme
D191N
-
lower activity compared to the wild type enzyme
D191N/H271A
-
lower activity compared to the wild type enzyme
H271A
-
lower activity compared to the wild type enzyme
H287A
-
lower activity compared to the wild type enzyme
S40A/T42A
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
structural and metabolic studies of bacterial and eucaryal phopholipids
Show AA Sequence (1127 entries)
Please use the Sequence Search for a specific query.