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Information on EC 2.4.1.217 - mannosyl-3-phosphoglycerate synthase
for references in articles please use BRENDA:EC2.4.1.217
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.217 mannosyl-3-phosphoglycerate synthase
IUBMB Comments
Requires Mg2+. The enzyme is absolutely specific for GDPmannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase), producing mannosylglycerate.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 2.4.1.217
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mannosylglycerate
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cavernous
- d-3-phosphoglycerate
-
osmoadaptation
-
intracavernosal
-
supra-annular
-
bioprostheses
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neurography
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thermoadaptation
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patient-prosthesis
-
rhodothermus
Reaction Schemes
showSynonyms
mpgs, mannosyl-3-phosphoglycerate synthase, mpg synthase, mannosyl-3-phosphoglycerate synthase/phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mannosyl-3-P-glycerate synthase
-
-
-
-
mannosyl-3-phosphoglycerate phosphatase
mannosyl-3-phosphoglycerate synthase
MPG synthase
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-
-
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MPGP
MPGS
synthase, mannosyl-3-phosphoglycerate
-
-
-
-
MPGS
-
-
-
-
MPGS
-
mannosyl-3-phosphoglycerate synthase domain of the bifunctional enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
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-
GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is bifunctional exhibiting both mannosyl-3-phosphoglycerate synthase, EC 2.4.1.217, and mannosyl-3-phosphoglycerate phosphatase, EC 3.1.3.70, activities, catalyzing the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis
-
GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
front-face SNi-like reaction mechanism, detailed overview. The binding of GDP-mannose:Mn2+ to the enzyme from Rhodothermus marinus induces significant conformational changes in the flexible loop. In particular, Tyr220 plays a pivotal role both in D-glycerate binding and in catalysis: it is reoriented towards the pocket interior and either interacts with the a phosphate of GDP-mannose
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GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
front-face SNi-like reaction mechanism, overview
-
GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
front-face SNi-like reaction mechanism, overview
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mannosylglycerate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:3-phospho-D-glycerate 3-alpha-D-mannosyltransferase
Requires Mg2+. The enzyme is absolutely specific for GDPmannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase), producing mannosylglycerate.
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CAS REGISTRY NUMBER
COMMENTARY
393512-63-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-glucosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: the enzyme is absolute specific for GDP-mannose and 3-phospho-D-glycerate as substrates
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
Products: -
Products: -
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GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: the enzyme is highly specific for the substrates GDP-mannose and 3-phospho-D-glycerate
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: the enzyme is highly specific for the substrates GDP-mannose and 3-phospho-D-glycerate
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
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Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
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Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: 2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
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Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: -
Products: -
Products: -
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
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Substrates: involved in a pathway for synthesis of mannosylglycerate
Products: mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate
Products: mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
Substrates: involved in a pathway for synthesis of mannosylglycerate
Products: -
Products: -
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: transfer of the mannosyl group with retention of configuration
Products: -
Products: -
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
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Substrates: the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
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-
Substrates: substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
Substrates: the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: besides its physiological substrate D-glycerate, RmaMGS is also able to use D-lactate and glycolate as sugar acceptors, thus displaying some acceptor plasticity. Substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. The enzyme from Rubrobacter xylanophilus is promiscuous and produces the phosphorylated form of glucosylglycerate (GPG) from GDP-glucose plus 3-D-phosphoglycerate with high efficiency. In spite of the less favorable parameters for the synthesis of mannosylglycerate, this is the only free glyceryl glycoside found in Rubrobacter xylanophilus cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly specific for 3-phospho-D-glycerate
Products: -
Products: -
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Substrates: the enzyme is highly specific for 3-phospho-D-glycerate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-glucose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-glucosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: 2 pathways for mannosylglycerate biosynthesis, a one-step and a two-step pathway, with specialized roles in osmoadaptation and thermoadaptation, the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress, regulatory mechanisms, overview
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Substrates: -
Products: -
Products: -
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Substrates: -
Products: -
Products: -
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
Substrates: involved in a pathway for synthesis of mannosylglycerate
Products: mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate
Products: mannosyl-3-phosphoglycerate is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
Substrates: involved in a pathway for synthesis of mannosylglycerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
Substrates: the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
Products: -
Products: -
?
additional information
?
-
-
Substrates: the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. The enzyme from Rubrobacter xylanophilus is promiscuous and produces the phosphorylated form of glucosylglycerate (GPG) from GDP-glucose plus 3-D-phosphoglycerate with high efficiency. In spite of the less favorable parameters for the synthesis of mannosylglycerate, this is the only free glyceryl glycoside found in Rubrobacter xylanophilus cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
Products: -
Products: -
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Substrates: all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
Mg2+
strictly dependent on, effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
Mg2+
activity is strictly dependent on divalent cations, Mn2+ is most effective (between 0.2 and 2.0 mM), Mg2+x01has a similar effect on the activation at about 20.0 mM
Mg2+
used as single metal cofactor at 20 mM, activity dependend on
Mn2+
effect of divalent cations on MpgS activity decreases in the following order Mg2+, Co2+, Mn2+
Mn2+
activity is strictly dependent on divalent cations, Mn2+ is most effective, maximum activation of the enzyme by Mn2+ is between 0.2 and 2.0 mM
additional information
-
enzyme requires divalent cations, Co2+ is preferred and can partially be substituted by Mg2+ or Mn2+, no activation by other cations
additional information
strictly dependent on divalent cations, no activation by Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+
additional information
-
strictly dependent on divalent cations, no activation by Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+
additional information
Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate activity at any concentration
additional information
-
Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate activity at any concentration
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
measurement in the presence of Zn2+ (300 microM) instead Mg2+, the activity decreases about 100fold (0.4 micromol/min/mg), Zn2+ can displace Mg2+ at the second metal binding site
additional information
no inhibition by 2-(alpha-D-mannosyl)-3-phosphoglycerate or mannosylglycerate
-
additional information
-
no inhibition by 2-(alpha-D-mannosyl)-3-phosphoglycerate or mannosylglycerate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress
-
additional information
-
the isozyme involved in the two-step pathway is upregulated by osmotic stress, the isozyme involved in the one-step pathway is upregulated by heat stress
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Calcinosis
Reconstruction and rendering of microcalcifications from two mammogram views by modified projective grid space (MPGS).
Carcinoma, Hepatocellular
Echo planar MR imaging of the liver: comparison of images with and without motion probing gradients.
Cysts
Echo planar MR imaging of the liver: comparison of images with and without motion probing gradients.
Hemangioma
Echo planar MR imaging of the liver: comparison of images with and without motion probing gradients.
Liver Neoplasms
Assessing Transcription Regulatory Elements To Evaluate the Expression Status of Missing Protein Genes on Chromosomes 11 and 19.
Neoplasm Metastasis
Echo planar MR imaging of the liver: comparison of images with and without motion probing gradients.
Neuroinflammatory Diseases
Increased Level of Tumor Necrosis Factor-Alpha (TNF-?) Leads to Downregulation of Nitrergic Neurons Following Bilateral Cavernous Nerve Injury and Modulates Penile Smooth Tone.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.81
3-phospho-D-glycerate
A164S/A208S/F211Y mutant, with GDP-mannose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
when 20 mM Mg2+ is added in combination with Zn2+ (300 microM), the MpgS specific activity recovered substantially
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4 - 7.4
7 - 8
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
pH-profile, 30-40% of maximal activity at pH 5.0 and pH 9.0
6 - 8
6 - 8
pH 6.0: about 40% of maximal activity, pH 8.0: about 40% of maximal activity
6 - 8
-
pH 6.0: about 60% of maximal activity, pH 8.0: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 75
80 - 90
90
90 - 100
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 103
25°C: 10% of the maximal activity, 103°C: 55% of maximal activity
50 - 100
temperature-profile, 10% of maximal activity at 25°C, 55% of maximal activity at 103°C
80 - 100
80 - 105
-
80°C: about 60% of maximal activity, 105°C: about 70% of maximal activity
80 - 100
80°C: about 60% of maximal activity, 100°C: about 60% of maximal activity
80 - 100
80°C: about 55% of maximal activity, 100°C: about 60% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
