Information on EC 3.1.3.85 - glucosyl-3-phosphoglycerate phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.85
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RECOMMENDED NAME
GeneOntology No.
glucosyl-3-phosphoglycerate phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O = 2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glucosylglycerate biosynthesis I
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glycolate and glyoxylate degradation
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucosyl-3-phospho-D-glycerate phosphohydrolase
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (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 glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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A9QXB5
UniProt
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
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
show the reaction diagram
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucosyl)-D-glycerate + phosphate
show the reaction diagram
A9QXB5
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-glucopyranosyl)-D-glycerate in one-step from 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-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
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?
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-mannopyranosyl)-D-glycerate + phosphate
show the reaction diagram
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
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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
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
show the reaction diagram
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucosyl)-D-glycerate + phosphate
show the reaction diagram
A9QXB5
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-glucopyranosyl)-D-glycerate in one-step from 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-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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at 30°C, GpgP retains 37% of its enzyme activity towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate and 12% activity towards 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate in a reaction mixture without cations compared to the activity with 10 mM K+ and Co2+. Potassium chloride, in the concentration range of 10 to 100 mM, stimulates enzyme activity about 40% at 50°C, but only when 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate is the substrate. However, at 30°C, K+ has a stimulatory effect towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate, but not with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate as the substrate
Ni2+
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at 50°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. Mg2+ and, to a lesser extent, Ni2+ can replace Co2+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 1.1
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
0.11 - 0.9
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9
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pH 4.5: about 40% of maximal activity, pH 9.0: about 45% of maximal activity, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
5.3 - 7.5
A9QXB5
pH 5.3: about 60% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate as substrate, pH 8.5: about 35% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate as substrate, about 80% of maximal activity with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
60
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substrate: 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
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30°C: about 55% of maximal activity, 70°C: about 50% of maximal activity, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
50 - 70
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50°C: about 60% of maximal activity, 70°C: about 60% of maximal activity, substrate: 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
60 - 100
A9QXB5
60°C: about 30% of maximal activity with 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate as substrate, about 50% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate as substrate, 100°C: about 15% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate as substrate
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31200
A9QXB5
1 * 31200, calculated from sequence
39160
A9QXB5
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
A9QXB5
1 * 31200, calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of apo-, vanadate-bound, and phosphate-bound MtbGpgP are refined to 1.95 A, 2.3 A and 1.77 A, respectively. Enzyme consists of a single domain made up of a central beta-sheet flanked by alpha-helices on either side. The active site is located in a positively charged cleft situated above the central beta-sheet
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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half-life: 198 h
23
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half-life: 165 h
50
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half-life: 12 min
70
A9QXB5
half-life: 462 min
85
A9QXB5
half-life: 12 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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recombinant GpgS protein
A9QXB5
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
overexpressed as His-tagged proteins in Escherichia coli
A9QXB5
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E84Q
mutant shows only 40% of catalytic activity compared to wild-type
H159A
mutation almost completely abolishes catalytic activity
L209E
mutation results in monomeric GpgP, rendering the enzyme incapable of dephosphorylation. Mutation almost completely abolishes catalytic activity
N17A
mutation almost completely abolishes catalytic activity
Q23A
mutant shows only 20% of catalytic activity compared to wild-type
R10A
mutation almost completely abolishes catalytic activity
R60A
mutation almost completely abolishes catalytic activity