5.3.1.8: mannose-6-phosphate isomerase
This is an abbreviated version!
For detailed information about mannose-6-phosphate isomerase, go to the full flat file.
Word Map on EC 5.3.1.8
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5.3.1.8
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phosphomannomutase
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gdp-mannose
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pyrophosphorylase
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phosphoglucomutase
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fructose-6-phosphate
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phosphoglucose
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enteropathy
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carbohydrate-deficient
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viannia
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allozyme
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braziliensis
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chlorophenol
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mannose-containing
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man-6-p
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phosphoglucoisomerase
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biolistic
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protein-losing
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l-ribose
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peruviana
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synthesis
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thermodenitrificans
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guyanensis
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biotechnology
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agriculture
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pharmacology
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analysis
- 5.3.1.8
- phosphomannomutase
- gdp-mannose
-
pyrophosphorylase
- phosphoglucomutase
- fructose-6-phosphate
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phosphoglucose
- enteropathy
-
carbohydrate-deficient
- viannia
-
allozyme
- braziliensis
- chlorophenol
-
mannose-containing
-
man-6-p
- phosphoglucoisomerase
-
biolistic
-
protein-losing
- l-ribose
- peruviana
- synthesis
- thermodenitrificans
-
guyanensis
- biotechnology
- agriculture
- pharmacology
- analysis
Reaction
Synonyms
BceA, BceAJ, becA, CHLNCDRAFT_139231, D-mannose-6-phosphate ketol-isomerase, GTMpi, Isomerase, mannose phosphate, KB1_0553, M6PI, ManA, Mannose phosphate isomerase, mannose-6-phosphate isomerase, MPI, Os01g0127900, Os09g0389000, PH0925, Phosphohexoisomerase, Phosphohexomutase, Phosphomannoisomerase, Phosphomannose isomerase, phosphomannose-isomerase, Phosphphexomutase, PMI, PMI/GMP, Pmi1, PMI2, PslB, type I phosphomannose isomerase, type I PMI
ECTree
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Metals Ions
Metals Ions on EC 5.3.1.8 - mannose-6-phosphate isomerase
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Ca2+
Co2+
Cu2+
Fe2+
Mg2+
Mn2+
Ni2+
Zinc
Zn2+
additional information
Ca2+
best activator, may be replaced by Mg2+ or Mn2+ for phosphomannose isomerase activity
Ca2+
divalent ions are necessary for PMI maximal activity in decreasing order of activation: Ca2+, Mn2+, Mg2+, Co2+, Ni2+
Co2+
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most effective activator of EDTA-inactivated enzyme, 1.7fold activation at 0.5 mM compared to initial activity
Co2+
divalent ions are necessary for PMI maximal activity in decreasing order of activation: Ca2+, Mn2+, Mg2+, Co2+, Ni2+
Cu2+
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maximal activity of the recombinant enzyme for L-ribulose isomerization in the presence of 0.5 mM Cu2+
Mg2+
60% of activity with Ca2+ for phosphomannose isomerase activity
Mg2+
divalent ions are necessary for PMI maximal activity in decreasing order of activation: Ca2+, Mn2+, Mg2+, Co2+, Ni2+
Mg2+
best activating divalent metal ion
Mn2+
65% of activity with Ca2+ for phosphomannose isomerase activity
Mn2+
divalent ions are necessary for PMI maximal activity in decreasing order of activation: Ca2+, Mn2+, Mg2+, Co2+, Ni2+
Ni2+
divalent ions are necessary for PMI maximal activity in decreasing order of activation: Ca2+, Mn2+, Mg2+, Co2+, Ni2+
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recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
Zinc
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enzyme contains an essential zinc atom. Four of the five ligands come from the protein, one of these ligands is unique in that it is a glutamine
Zinc
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recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
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at low concentrations complete reactivation of enzyme inhibited by a metal binding agent
Zn2+
The Zn binding mode of the 5-phospho-D-arabinonhydrazide inhibitor mimics the bidentate Zn coordination of substrate and high energy intermediate
Zn2+
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noncovalent complexation, ESI-FTICR study, binding/release of metal ion changes substrate binding affinity by at least 5fold
Zn2+
enzyme-bound, Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site
Zn2+
Zn2+ is present at one molecule per monomer, the enzyme has about 240% activity in the presence of 0.5 mM Zn2+
mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis
additional information
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mannose-6-phosphate isomerases are metalloenzymes that require a divalent ion metal cofactor for activity and catalysis
additional information
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the enzyme requires divalent cations for activity
additional information
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activated by bivalent cations in the order: Co2+, Ni2+, Mn2+, Mg2+, Ca2+, Zn2+
additional information
divalent cations are absolutely required for activity, metal binding increases the thermostability of the enzyme
additional information
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divalent cations are absolutely required for activity, metal binding increases the thermostability of the enzyme
additional information
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PMI absolutely requires divalent metal cations for catalytic activity
additional information
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the enzyme is not affected by Ca2+, Mg2+, Ba2+, and Ni2+
additional information
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activated by bivalent cations in decreasing order: Co2+, Zn2+, Mn2+, Ni2+, Ca2+