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
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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
5.3.1.8 mannose-6-phosphate isomeraseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 5.3.1.8 - mannose-6-phosphate isomerase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Ag+
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irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme
GDP-D-mannose
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inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway
p-chloromercuribenzoate
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0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity
S-nitroso-acetyl-penicillamine
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dose- and time-dependent inactivation
5-phospho-D-arabinonohydroxamic acid
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in 50 mM HEPES buffer, pH 7.1, at 25°C; nanomolar inhibitor
5-phospho-D-arabinonohydroxamic acid
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50% inhibition at 0.000169 mM, inhibition of both type I and type II isozymes
5-phospho-D-arabinonohydroxamic acid
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50% inhibition at 0.000136 mM, inhibition of both type I and type II isozymes
benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
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benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside
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benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose
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dithiothreitol
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1 mM, 73% residual activity; 1 mM, 84% residual activity
EDTA
no activity is detected when 2 mM EDTA is added to the dialysis buffer
EDTA
complete inhibition at 1 mM, reversible by the addition of divalent metal cations such as Zn2+, Mn2+, Co2+, Mg2+ and Ni2+
Hg2+
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partial noncompetitive inhibition with mannose 6-phosphate as substrate. In addition to the inhibition at rapid equilibrium, inactivation occurs in a two-step process, proceeding via an intermediate complex. The rate of the irreversible inactivation can be slowed by the addition of the substrate mannose 6-phosphate
Hg2+
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competitive, relatively pH-independent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion
Silver sulfadiazine
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wild-type enzyme is inhibited, mutant enzyme Cys150Ala is not inhibited
Zn2+
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inhibitory to both phosphomannose isomerase and guanosine diphosphate-D-mannose diphosphorylase activities
Zn2+
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competitive with mannose 6-phosphate, strongly pH-dependent. Zn2+ and Hg2+ can simultaneously bind in the mannose 6-phosphate binding pocket, with only a small mutual repulsion
additional information
not inhibitory: mannose 1-phosphate, GTP, GDP-mannose, or diphosphate
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additional information
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not inhibitory: mannose 1-phosphate, GTP, GDP-mannose, or diphosphate
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additional information
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synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive enzyme inhibitors. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview
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additional information
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synthesis of a non-hydrolyzable D-mannose 6-phosphate surrogates as strong competitive inhibitors of the enzyme. Effective binding to the catalytic site occurs with retention of the Zn(II)-bound water molecule. Molecular mechanics study of enzyme substrate and inhibitors, overview
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additional information
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no inhibition by GTP, mannose 1-phosphate, and phosphodiphosphate
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