Information on EC 2.4.1.266 - glucosyl-3-phosphoglycerate synthase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.4.1.266
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RECOMMENDED NAME
GeneOntology No.
glucosyl-3-phosphoglycerate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NDP-glucose + 3-phospho-D-glycerate = NDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucosylglycerate biosynthesis I
-
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mannosylglucosylglycerate biosynthesis I
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glycolate and glyoxylate degradation
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SYSTEMATIC NAME
IUBMB Comments
NDP-glucose:3-phospho-D-glycerate 2-alpha-D-glucosyltransferase
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor [1]. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate [2]. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria [4,5].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
slow-growing strain BCG, gene gpgS; strain BCG
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-
Manually annotated by BRENDA team
fast-growing strain 1102, gene gpgS; strain 1102
SwissProt
Manually annotated by BRENDA team
strain 1102
SwissProt
Manually annotated by BRENDA team
strain H37Rv, gene gpgS or Rv1208
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain SS120
UniProt
Manually annotated by BRENDA team
strain SS120
UniProt
Manually annotated by BRENDA team
strain PCC 7002
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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construction of a MSMEG_5084 knock-out mutant. As compared to its wild-type strain, the knock-out mutant strain mutant displays a significantly reduced growth rate at 37C. Virtual elimination of the de novo production of methylglucose lipopolysaccharides molecules in the mutant
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-alpha-D-glucose + D-3-phosphoglycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
ADP-glucose + 3-phospho-D-glycerate
ADP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
show the reaction diagram
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
GDP-glucose + D-3-phosphoglycerate
GDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
show the reaction diagram
-
-
-
?
TDP-glucose + 3-phospho-D-glycerate
TDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
the recombinant GpgS protein of Persephonella marina catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate
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-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
show the reaction diagram
in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucosyl)-D-glycerate in one-step fop, ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
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-
?
UDP-glucose + D-3-phosphoglycerate
UDP + 2-(beta-D-glucosyl)-sn-glycerol 3-phosphate
show the reaction diagram
additional information
?
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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
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
Q12XX4
synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). An mpgS gene coding for mannosyl-3-phosphoglycerate synthase (MpgS) is absent
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-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
A9BHI9
the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation
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-
?
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
show the reaction diagram
UDP-glucose + 3-phospho-D-glycerate
UDP + 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate
show the reaction diagram
A9QXB4
in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucosyl)-D-glycerate in one-step fop, ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
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-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) is dependent on divalent cations for activity: Co2+, Mn2+, Ni2+, Mg2+, and Zn2+. Co2+ (5 mM) has a more pronounced stimulatory effect
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phospho-D-glycerate
ADP
strong inhibtor
UMP
-
competitive with UDP-glucose, uncompetitive with 3-phospho-D-glycerate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09 - 8
3-phospho-D-glycerate
0.7 - 6.63
ADP-glucose
1.75 - 32.04
GDP-glucose
0.48 - 20
UDP-glucose
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.83
UDP-glucose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 3.58
3-phospho-D-glycerate
201
0.024 - 1.28
UDP-glucose
64
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21
3-phospho-D-glycerate
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substrate UDP-glucose, pH 7.8, 25C
0.21 - 0.22
UMP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
substrate GDP-glucose, pH 7.5, 25C
0.0629
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with GDP-glucose as a substrate
0.17
substrate UDP-glucose, pH 7.5, 25C
1.1
substrate ADP-glucose, pH 7.5, 25C
5
substrate: TDP-glucose, pH 8.0, 90C
10
substrate: ADP-glucose, pH 8.0, 90C
41
substrate: GDP-glucose, pH 8.0, 90C
94
substrate: UDP-glucose, pH 8.0, 90C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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activity range
6 - 9
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pH 6.0: about 50% of maximal activity, pH 9.5: about 75% of maximal activity
6 - 10
activity range
6 - 9.5
pH 6.0: about 55% of maximal activity, pH 9.5: about 60% of maximal activity
6 - 8
pH 6.0: about 80% of maximal activity, pH 8.0: about 50% of maximal activity
6.5 - 9.5
pH 6.5: about 55% of maximal activity, pH 9.5: about 70% of maximal activity
7.5 - 9.5
pH 7.5: about 60% of maximal activity, pH 9.5: about 80% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
30 - 70
30C: about 50% of maximal activity, 70C: about 50% of maximal activity
30 - 50
30C: about 40% of maximal activity, 50C: about 70% of maximal activity
35 - 50
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30C: about 35% of maximal activity, 35C: about 60% of maximal activity, 50C: about 90% of maximal activity, 55C: about 25% of maximal activity
60 - 100
the enzyme is inactive at 40C, 60C: about 60% of maximal activity, 100C: 33% of maximal activity
60 - 75
60C: about 85% of maximal activity, 75C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33900
3 * 33900, calculated from sequence
34400
-
3 * 34400, calculated from sequence
37100
2 * 37100, calculated from sequence
43000
x * 43000, calculated from sequence
44990
5 * 44990, calculated
46700
2 * 46700, calculated from sequence
80000
gel filtration
101100
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gel filtration
105400
gel filtration
106900
gel filtration
218600
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 43000, calculated from sequence
pentamer
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme in the presence of the sugar donor UDP-Glc, the acceptor substrate phosphoglycerate, and the divalent cation cofactor forms a native ternary complex. The catalytic mechanism is a front-side substrate-assisted SNi-type reaction
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hanging-drop vapour diffusion method at 20C, three-dimensional structure of the apoenzyme, as well as of its ternary complex with UDP and 3-phosphoglycerate is determined by X-ray crystallography, to a resolution of 2.5 and 2.7 A, respectively
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
half-life: 11.5 h
50
half-life: 13.8 h
60
half-life: 6 min, addition of Co2+ had a negligible stabilizing effect, addition of both substrates increased the half-life of the enzyme to about 16 min
70
half-life is 14 min
90
half-life is 2.3 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, purified recombinant enzyme, nearly 100% remaining activity after 1 month
22C, room temperature, purified recombinant enzyme, nearly 100% remaining activity after 1 week
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
recombinant enzyme from Escherichia coli; recombinant GpgS protein
recombinant GpgS protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli
gene gpgS, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3), the genes for glucosyl-3-phosphoglycerate synthase, GpgS, and glucosyl-3-phosphoglycerate phosphatase, GpgP, the enzymes that lead to the synthesis of glucosylglycerol through the formation of glucosyl-3-phosphoglycerate, are organized in anoperon-like structure with the gene encoding a putative glycosyltransferase, the glucosylglycerate synthase, Ggs, overview
gene gpgS, DNA and amino acid sequence determination and analysis, phylogenetic tree
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gene gpgS, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression in Escherichia coli strain BL21; overexpressed in Escherichia coli as a C-terminal His-tagged protein
overexpressed as His-tagged proteins in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D134A
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substitution of a canonical GT-A D134XD136 aspartic acid, complete loss of activity
D136A
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substitution of a canonical GT-A D134XD136 aspartic acid, complete loss of activity
E232A
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kinetic parameters similar to wild-type
H258A
-
2540-fold increases in Km values
R256A
-
mutation in a flexible loop covering the active site, strong increase in Km values
R261A
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kinetic parameters similar to wild-type
T187A
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100fold decrease in the value of kcat
D134A
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substitution of a canonical GT-A D134XD136 aspartic acid, complete loss of activity
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D136A
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substitution of a canonical GT-A D134XD136 aspartic acid, complete loss of activity
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E232A
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kinetic parameters similar to wild-type
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H258A
-
2540-fold increases in Km values
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R256A
-
mutation in a flexible loop covering the active site, strong increase in Km values
-
Show AA Sequence (146 entries)
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