Information on EC 3.1.3.70 - mannosyl-3-phosphoglycerate phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.70
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RECOMMENDED NAME
GeneOntology No.
mannosyl-3-phosphoglycerate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2(alpha-D-mannosyl)-D-glycerate + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphate bond
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Fructose and mannose metabolism
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mannosylglycerate biosynthesis I
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mannosylglycerate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannosyl-3-phosphoglycerate phosphohydrolase
Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for alpha-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.
CAS REGISTRY NUMBER
COMMENTARY hide
393512-74-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
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two distinct enzyme conformations, open and closed, are catalytically relevant: the apo-MpgP is prevalently found in the open state, while the holo-MpgP, in complex with the reaction products, is found in the closed state. Enzyme activation entails a structural rearrangement of Motifs I and IV with concomitant binding of the co-catalytic Mg2+ ion. The closure motion of the C2B domain is subsequently triggered by the anchoring of the phosphoryl group to the co-catalytic metal center, and by Arg167 fixing the mannosyl moiety inside the catalytic pocket
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
show the reaction diagram
2-(alpha-D-glucosyl)-3-phosphoglycerate + H2O
2-(alpha-D-mannosyl)-D-glycerate + phosphate
show the reaction diagram
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ir
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(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.134
2(alpha-D-mannosyl)-3-phosphoglycerate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2 - 7.5
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pH 4.2: 60% of maximal actuvity, pH 7.5: about 45% of maximal activity
5 - 7.5
pH 6.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 100
70°C: about 55% of maximal activity, 100°C: about 70% of maximal activity
70 - 108
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70°C: about 45% of maximal activity, 108°C: about 20% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27100
x * 27100, SDS-PAGE
27130
x * 27130, calculated from sequence
28200
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2 * 28200, recombinant enzyme, SDS-PAGE
56400
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recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 28200, recombinant enzyme, SDS-PAGE
additional information
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detailed structure analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo enzyme form lacking magnesium ions using the multiple-wavelength anomalous diffraction method and magnesium-bound holo enzyme form using the molecular-replacement method, with 16-20% (w/v) PEG 3350, 0.2 M ammonium chloride and 0.1 M MES-NaOH pH 6.0
purified recombinant enzyme in apo-form and in complex with substrates, substrate analogues and inhibitors, sitting drop vapor diffusion technique, 10 mg/ml protein in 20 mM MES-NaOH pH 6.3, 760 mM NaCl, 5 mM DTT, 1 mM EDTA, 5 mM Mg2+ and Na/KPO4, is mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis, molecular replacement
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purified recombinant enzyme, sitting drop vapour diffusion technique, 10 mg/ml in 20 mM MES-NaOH, pH 6.35, 5 mM DTT, 1 mM EDTA, 5 mM MgCl2, and 760 mM NaCl, mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio forming 0.002 ml drops, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis at 1.90 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83
half-life: 25 min
98
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half-life: 15.6 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap Ni2+-chelating column chromatography, Source 15Q column chromatography, and Superdex 75 gel filtration
recombinant enzyme from Escherichia coli strain BL21 (DE3) by anion exchange and cation exchange chromatography
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recombinant enzyme from Escherichia coli strain BL21 (DE3) by cation exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli strain BL21 (DE3)
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