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Information on EC 2.4.1.217 - mannosyl-3-phosphoglycerate synthase
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EC Tree
2.4.1.217 mannosyl-3-phosphoglycerate synthaseIUBMB 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.
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Word Map
- 2.4.1.217
-
mannosylglycerate
-
cavernous
- d-3-phosphoglycerate
-
osmoadaptation
-
intracavernosal
-
supra-annular
-
bioprostheses
-
neurography
-
thermoadaptation
-
patient-prosthesis
-
rhodothermus
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
Synonyms
mpgs, mannosyl-3-phosphoglycerate synthase, mpg synthase, mannosyl-3-phosphoglycerate synthase/phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mannosyl-3-P-glycerate synthase
-
-
-
-
mannosyl-3-phosphoglycerate phosphatase
mannosyl-3-phosphoglycerate synthase
MPG synthase
-
-
-
-
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
-
-
-
-
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
-
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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PATHWAY SOURCE
PATHWAYS
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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
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
-
-
-
-
?
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-alpha-D-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
the enzyme is absolute specific for GDP-mannose and 3-phospho-D-glycerate as substrates
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is highly specific for the substrates GDP-mannose and 3-phospho-D-glycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is highly specific for the substrates GDP-mannose and 3-phospho-D-glycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
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
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
involved in a pathway for synthesis of mannosylglycerate
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
-
involved in a pathway for synthesis of mannosylglycerate
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
transfer of the mannosyl group with retention of configuration
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate binding structure, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
additional information
?
-
-
the enzyme is highly specific for 3-phospho-D-glycerate
-
-
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
the enzyme is highly specific for 3-phospho-D-glycerate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
the enzyme is involved in synthesis of mannosylglycerate
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
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
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
synthesis of mannosylglycerate proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70)
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
GDP-mannose + 3-phospho-D-glycerate
GDP + 2-(alpha-D-mannosyl)-3-phosphoglycerate
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
?
GDPmannose + 3-phospho-D-glycerate
GDP + 2-(1-D-mannosyl)-3-phosphoglycerate
-
involved in a pathway for synthesis of mannosylglycerate
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
-
involved in a pathway for synthesis of mannosylglycerate
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes the consecutive synthesis and dephosphorylation of mannosyl-3-phosphoglycerate in mannosylglycerate biosynthesis, enzyme evolution
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide increases the activity by 10fold
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
additional information
?
-
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
all MPGSs have high affinity for GDP-mannose and 3-D-phosphoglycerate. Substrate binding structure, overview
-
-
?
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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
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
AY193871, GenBank sequence encoding mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase
SwissProt
brenda
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
AY193871, GenBank sequence encoding mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase
SwissProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the enzyme is included in the glycosyltransferase family GT55
evolution
-
the promiscuous MPGS/GPGS from Rubrobacter xylanophilus (RxyMPGS) is included within the retaining GT81 family, members of the GT55 and GT81 families preserved a common structural core, defined by the alpha/beta/alpha region containing 7 beta-strands in the order 3-2-1-4-6-5-7, with beta6 antiparallel to the rest, that could be included into the MGS-like family
evolution
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
the enzyme is included in the glycosyltransferase family GT55
-
evolution
-
the enzyme is included in the glycosyltransferase family GT55
-
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS)catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
metabolism
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
-
metabolism
-
mannosylglycerate metabolism overview: pathways for the synthesis and hydrolysis of mannosylglycerate (MG). In the single-step pathway mannosylglycerate synthase (MGS) catalyzes the direct condensation of GDP-mannose with D-glycerate to produce MG. In the two-step pathway, mannosyl-3-phosphoglycerate synthase (MPGS) catalyzes the conversion of GDP-mannose and D-3-phosphoglycerate into mannosyl-3-phosphoglycerate (MPG) which is dephosphorylated into MG by mannosyl-3-phosphoglycerate phosphatase (MPGP)
-
physiological function
the enzyme is involved in synthesis of mannosylglycerate
physiological function
-
the enzyme is involved in synthesis of mannosylglycerate
-
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
-
additional information
-
the catalytic pocket of MPGS is solvent-exposed at the NDP-sugar binding region, allowing ready access of the substrate
-
Show AA Sequence and Transmembrane Helices (217 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43600
45584
x * 48795, isozyme 1, mass spectrometry, x * 45584, isozyme 2, mass spectrometry
48795
x * 48795, isozyme 1, mass spectrometry, x * 45584, isozyme 2, mass spectrometry
50000
-
x * 78000, recombinant bifunctional holoenzyme, SDS-PAGE, x * 50000, about, recombinant mannosyl-3-phosphoglycerate synthase domain, SDS-PAGE
78000
-
x * 78000, recombinant bifunctional holoenzyme, SDS-PAGE, x * 50000, about, recombinant mannosyl-3-phosphoglycerate synthase domain, SDS-PAGE
95000
determined by gel filtration, suggesting that it is dimeric in solution
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 78000, recombinant bifunctional holoenzyme, SDS-PAGE, x * 50000, about, recombinant mannosyl-3-phosphoglycerate synthase domain, SDS-PAGE
?
x * 48795, isozyme 1, mass spectrometry, x * 45584, isozyme 2, mass spectrometry
additional information
-
monomer structure from crystal structure modeling, overview
additional information
-
monomer structure from crystal structure modeling, overview
additional information
-
monomer structure from crystal structure modeling, overview
-
additional information
-
monomer structure from crystal structure modeling, overview
additional information
-
monomer structure from crystal structure modeling, overview
additional information
-
monomer structure from crystal structure modeling, overview
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
monomer structure from crystal structure modeling, overview
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the 30 amino acid C-terminal sequence of the enzyme has regulatory function, cleaving of this peptide by intracellular proteases increases the activity by 10fold
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the unliganded MpgS and of its complexes with the nucleotide and sugar donors, at 2.2, 2.8 and 2.5 A resolution respectively
for the native protein a data set extending to 2.20 A resolution is collected, for the mercury derivative a data set extending to 3.05 A, and for the ternary complex with GDP and mannose a data set extending to 2.80 A
hanging drop vapor diffusion method, using 0.2 M magnesium acetate, 0.1 M sodium cacodylate pH 6.5, 30-35% MPD with 600 mM ZnCl2, the addition of Zn2+ to the crystallization buffer is essential in order to obtain crystals
-
the three-dimensional structure of mannosyl-3-phosphoglycerate synthase in its binary complex form, with GDP-alpha-D-mannose and Mg2+, shows a second metal binding site, about 6 A away from the mannose moiety, wild-type and H309A mutant
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A164S/A208S/F211Y
MpgS triple mutant engineered to reinforce the hydrogen-bonding network
E251A
site-directed mutagenesis, no specific activity detected
H309A
site-directed mutagenesis with the absence of the metal site, negligible specific activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
80
83
90
98
additional information
100
85% remaining activity of the truncated enzyme, the full length enzyme is inactive
80
half-life truncated enzyme: 79 min, half-life full length enzyme: 40 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant monofunctional mannosyl-3-phosphoglycerate synthase domain is unstable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native isozymes in a multistep procedure, recombinant isozymes from Escherichia coli by 3 chromatographic steps of cation exchange chromatography and gel filtration
native mannosyl-3-phosphoglycerate synthase is purified from Rubrobacter xylanophilus cells using a Q-Sepharose FF and a Mono-Q column, recombinant MpgS is purified by immobilized metal-affinity chromatography on a Ni-Sepharose column
Q-Sepharose column chromatography, Resource Q column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, genetic organization of genes involved in mannosylglycerate biosynthesis, functional overexpression in Escherichia coli strain BL21
gene mgsD, DNA and amino acid sequence determination and analysis, genetic organization, overexpression of the holoenzyme and of the isolated mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase domains of the bifunctional enzyme in Escherichia coli, the recombinant Escherichia coli strain does not accumulate mannosylglycerate, expression of active bifunctional enzyme in Saccharomyces cerevisiae
-
gene mpgs, DNA and amino acid sequence determination and analysis of the 2 isozymes, expression in Escherichia coli strain BL21(DE)
into the pGEMT-Easy vector for sequencing and subcloned into pET30a for expression in Escherichia coli BL21DE3 cells
phylogenetic analysis
the mpgS gene from strain HB27 is cloned into the pGEM-T Easy vector
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martins, L.O.; Empadinhas, N.; Marugg, J.D.; Miguel, C.; Ferreira, C.; Da Costa, M.S.; Santos, H.
Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus. Biochemical and genetic characterization of a mannosylglycerate synthase
J. Biol. Chem.
274
35407-35414
1999
Rhodothermus marinus
brenda
Empadinhas, N.; Marugg, J.D.; Borges, N.; Santos, H.; Da Costa, M.S.
Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes
J. Biol. Chem.
276
43580-43588
2001
Pyrococcus horikoshii
brenda
Empadinhas, N.; Albuquerque, L.; Henne, A.; Santos, H.; da Costa, M.S.
The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate
Appl. Environ. Microbiol.
69
3272-3279
2003
Thermus thermophilus (Q84B24), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q84B24)
brenda
Empadinhas, N.; Albuquerque, L.; Costa, J.; Zinder, S.H.; Santos, M.A.; Santos, H.; da Costa, M.S.
A gene from the mesophilic bacterium Dehalococcoides ethenogenes encodes a novel mannosylglycerate synthase
J. Bacteriol.
186
4075-4084
2004
Dehalococcoides mccartyi, no activity in Saccharomyces cerevisiae
brenda
Borges, N.; Marugg, J.D.; Empadinhas, N.; da Costa, M.S.; Santos, H.
Specialized roles of the two pathways for the synthesis of mannosylglycerate in osmoadaptation and thermoadaptation of Rhodothermus marinus
J. Biol. Chem.
279
9892-9898
2004
Rhodothermus marinus (Q6WSQ4), Rhodothermus marinus
brenda
Neves, C.; da Costa, M.S.; Santos, H.
Compatible solutes of the hyperthermophile Palaeococcus ferrophilus: osmoadaptation and thermoadaptation in the order Thermococcales
Appl. Environ. Microbiol.
71
8091-8098
2005
Thermococcus litoralis (Q2VPR9), Thermococcus litoralis, Palaeococcus ferrophilus (Q2VPS1), Palaeococcus ferrophilus, Palaeococcus ferrophilus DSM 13482T (Q2VPS1)
brenda
Sa-Moura, B.; Albuquerque, L.; Empadinhas, N.; da Costa, M.S.; Pereira, P.J.; Macedo-Ribeiro, S.
Crystallization and preliminary crystallographic analysis of mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus
Acta Crystallogr. Sect. F
64
760-763
2008
Rubrobacter xylanophilus (B7SY86), Rubrobacter xylanophilus
brenda
Alarico, S.; Empadinhas, N.; Mingote, A.; Simoes, C.; Santos, M.S.; da Costa, M.S.
Mannosylglycerate is essential for osmotic adjustment in Thermus thermophilus strains HB27 and RQ-1
Extremophiles
11
833-840
2007
Thermus thermophilus (Q84B24), Thermus thermophilus
brenda
Goncalves, S.; Borges, N.; Santos, H.; Matias, P.M.
Crystallization and preliminary X-ray analysis of mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27
Acta Crystallogr. Sect. F
65
1014-1017
2009
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
Goncalves, S.; Borges, N.; Esteves, A.M.; Victor, B.L.; Soares, C.M.; Santos, H.; Matias, P.M.
Structural analysis of Thermus thermophilus HB27 mannosyl-3-phosphoglycerate synthase provides evidence for a second catalytic metal ion and new insight into the retaining mechanism of glycosyltransferases
J. Biol. Chem.
285
17857-17868
2010
Thermus thermophilus HB27 (Q84B24), Thermus thermophilus HB27
brenda
Empadinhas, N.; Pereira, P.J.; Albuquerque, L.; Costa, J.; S-Moura, B.; Marques, A.T.; Macedo-Ribeiro, S.; da Costa, M.S.
Functional and structural characterization of a novel mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus reveals its dual substrate specificity
Mol. Microbiol.
79
76-93
2011
Rubrobacter xylanophilus (B7SY86), Rubrobacter xylanophilus
brenda
Borges, N.; Jorge, C.D.; Goncalves, L.G.; Goncalves, S.; Matias, P.M.; Santos, H.
Mannosylglycerate: structural analysis of biosynthesis and evolutionary history
Extremophiles
18
835-852
2014
Palaeococcus ferrophilus, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Rhodothermus marinus, Rubrobacter xylanophilus, Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
Costa, J.; Empadinhas, N.; Goncalves, L.; Lamosa, P.; Santos, H.; Da Costa, M.
Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii
J. Bacteriol.
188
1022-1030
2006
Pyrococcus horikoshii (O58690), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58690)
brenda
Empadinhas, N.; Albuquerque, L.; Henne, A.; Santos, H.; Da Costa, M.
The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate
Appl. Environ. Microbiol.
69
3272-3279
2003
Thermus thermophilus (Q84B24), Thermus thermophilus, Thermus thermophilus DSM 7039 (Q84B24)
brenda
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