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

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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
-
-
-
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reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
CDP-archaeol biosynthesis
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lipid metabolism
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Glycerophospholipid metabolism
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KS8-1
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Manually annotated by BRENDA team
strain KS8-1
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-
Manually annotated by BRENDA team
strain HO-62
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-
Manually annotated by BRENDA team
strain HO-62
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-
Manually annotated by BRENDA team
Thermoplasma sp.
strain HO-62
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Manually annotated by BRENDA team
strain HO-62
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-
Manually annotated by BRENDA team
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
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
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-
-
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
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-
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
K+
-
maximum activity at 60-80 mM
Na+
-
maximum activity 20-25 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
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slight inhibition at 1 mM
Cu2+
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slight inhibition at 1 mM
DTT
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45% inhibition at 1 mM
K+
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slight inhibition at 70 mM
Na+
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slight inhibition at 70 mM
NAD(P)+
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competitive with NAD(P)H and noncompetitive with dihydroxyacetone phosphate
Ni2+
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slight inhibition at 1 mM
sn-glycerol-1-phosphate
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noncompetitive with dihydroxyacetone phosphate and NAD(P)H
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
0.025 - 0.165
NADPH
8.92
sn-glycerol-1-phosphate
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pH 7.0, 65C
additional information
additional information
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kinetic analysis
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.493 - 60.47
dihydroxyacetone phosphate
0.09
NAD+
Aeropyrum pernix
-
pH 7.0, 65C
2.4
NADH
Aeropyrum pernix
-
pH 7.0, 65C
0.044
NADPH
Aeropyrum pernix
-
pH 7.0, 65C
0.09
sn-glycerol-1-phosphate
Aeropyrum pernix
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pH 7.0, 65C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.22
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purified enzyme, pH 7.0, 65C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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in MES buffer or MOPS buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 7.7
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
94 - 96
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 85
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at temperatures higher than 85C no activity of the enzyme can be detected due to precipitation
55 - 96
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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
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SDS-PAGE
72400
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 38000, SDS-PAGE
monomer
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octamer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
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decrease of activity below
207960
6.8
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at pH 6.8 86-91% of activity is detected
668020
7.4
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decrease of activity above
207960
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51
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temperature-induced conformational change
90
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half-life: 2 h
95
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half-life: 0.5 h
96
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
to homogeneity, 7step chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
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expression in Escherichia coli
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phylogenetic analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144A
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lower activity compared to the wild type enzyme
D144N
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lower activity compared to the wild type enzyme
D191N
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lower activity compared to the wild type enzyme
D191N/H271A
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lower activity compared to the wild type enzyme
H271A
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lower activity compared to the wild type enzyme
H287A
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lower activity compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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structural and metabolic studies of bacterial and eucaryal phopholipids
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