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
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carbohydrate-deficient
- viannia
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allozyme
- braziliensis
- chlorophenol
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mannose-containing
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man-6-p
- phosphoglucoisomerase
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biolistic
-
protein-losing
- l-ribose
- peruviana
- synthesis
- thermodenitrificans
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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
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results (Engineering
Engineering on EC 5.3.1.8 - mannose-6-phosphate isomerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C150A
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mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition
L129F
the activity of the mutant is 204% of the activity of the wild type enzyme
L129W
the activity of the mutant is 10% of the activity of the wild type enzyme
L129Y
the activity of the mutant is 94% of the activity of the wild type enzyme
N90A/L129F
the activity of the mutant is about 6fold higher than the activity of the wild type enzyme
W17Q/N90A/L129F
R408A
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complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
R408K
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complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity
D138A
E132A
E132D
the mutant shows 0.4% activity compared to the wild type enzyme
E67A
E67D
the mutant shows 3.7% activity compared to the wild type enzyme
E67Q
the mutant shows 0.8% activity compared to the wild type enzyme
H122A
H122Q
the mutant shows 2.0% activity compared to the wild type enzyme
H50A
H50Q
the mutant shows 2.0% activity compared to the wild type enzyme
K37A
K65A
L18A
L39A
Q48A
R11A
R142A
R142K
R142N
W13A
W13F
the mutant shows 41% activity compared to the wild type enzyme
W13H
the mutant shows 52% activity compared to the wild type enzyme
W13Y
the mutant shows 68% activity compared to the wild type enzyme
W69A
Y124A
the mutant shows 52% activity compared to the wild type enzyme
E132A
E132D
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the mutant shows 0.4% activity compared to the wild type enzyme
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H122A
K37A
R11A
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the enzyme shows about wild type specific activity for L-ribulose
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R142K
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the enzyme shows decreased specific activity for L-ribulose
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additional information
W17Q/N90A/L129F
the specific activity and catalytic efficiency for L-ribulose isomerization of this variant are 3.1 and 7.1fold higher, respectively, than those of the wild type enzyme at pH 7.0 and 70°C in the presence of 1mM Co2+
D138A
the mutant shows 59% activity compared to the wild type enzyme
E132A
the mutant shows 1.9% activity compared to the wild type enzyme
E67A
the mutant shows 2.5% activity compared to the wild type enzyme
H122A
the mutant shows 2.8% activity compared to the wild type enzyme
H50A
the mutant shows 2.2% activity compared to the wild type enzyme
K37A
the mutant shows 21% activity compared to the wild type enzyme
K65A
the mutant shows 15% activity compared to the wild type enzyme
L18A
the mutant shows 78% activity compared to the wild type enzyme
L39A
the mutant shows 84% activity compared to the wild type enzyme
Q48A
the mutant shows 2.0% activity compared to the wild type enzyme
R11A
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the enzyme shows about wild type specific activity for L-ribulose
R11A
the mutant shows 260% activity compared to the wild type enzyme
R142A
the mutant shows 2.6% activity compared to the wild type enzyme
R142N
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the specific activity and catalytic efficiency (kcat/Km) for L-ribulose using the R142N mutant are 1.4 and 1.6fold higher than those of the wild type enzyme, respectively
W13A
the mutant shows 0.4% activity compared to the wild type enzyme
W69A
the mutant shows 50% activity compared to the wild type enzyme
E132A
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the mutant shows 1.9% activity compared to the wild type enzyme
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H122A
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the mutant shows 2.8% activity compared to the wild type enzyme
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K37A
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the enzyme shows decreased specific activity for L-ribulose
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K37A
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the mutant shows 21% activity compared to the wild type enzyme
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additional information
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knockout of isoform Pmi2 does not affect the total ascorbic acid levels in leaves
additional information
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reduction of Pmi1 expression by RNA interference results in substantial decrease in the total ascorbic acid content of leaves
additional information
construction of a DELTApmi1 enzyme knockout mutant cell, that shows a significantly reduced growth rate at a high concentration of Man. Both inadequate and replete Man leads to an accumulation of intracellular Man-6-P and a reduction in the amount of alpha-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
additional information
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construction of a DELTApmi1 enzyme knockout mutant cell, that shows a significantly reduced growth rate at a high concentration of Man. Both inadequate and replete Man leads to an accumulation of intracellular Man-6-P and a reduction in the amount of alpha-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
additional information
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construction of a DELTApmi1 enzyme knockout mutant cell, that shows a significantly reduced growth rate at a high concentration of Man. Both inadequate and replete Man leads to an accumulation of intracellular Man-6-P and a reduction in the amount of alpha-glucan in the cell wall. Uncoupling of the link between energy production and glycosylation by deletion of the pmi1 gene leads to phenotypes such as defects in cell wall integrity, abnormal morphology and reduced conidiation, overview
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additional information
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transformation of Brassica napus with gene pmi as a selectable marker, transformation via Agrobacterium tumefaciens in hypocotyl explants, overview
additional information
enzyme-deficient mutant is not impaired in synthesis of exopolysaccharide. However, the viscosity of aqueous solutions prepared with the exopolysaccharide produced by the mutant is significantly reduced compared with wild-type biopolymer and the mutant forms biofilms with a size reduced by 6fold
additional information
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enzyme-deficient mutant is not impaired in synthesis of exopolysaccharide. However, the viscosity of aqueous solutions prepared with the exopolysaccharide produced by the mutant is significantly reduced compared with wild-type biopolymer and the mutant forms biofilms with a size reduced by 6fold
additional information
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enzyme-deficient mutant is not impaired in synthesis of exopolysaccharide. However, the viscosity of aqueous solutions prepared with the exopolysaccharide produced by the mutant is significantly reduced compared with wild-type biopolymer and the mutant forms biofilms with a size reduced by 6fold
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additional information
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ablation of enzyme gene, homozygous embryos die around E11.5. Supplementation with D-mannose hastened their death. Embryos show growth retardation and placental hyperplasia. More than 90% of embryos failed to form yolk sac vasculature, and 35% failed chorioallantoic fusion
additional information
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point mutation at nucleotide 961 greatly decreases enzyme activity
additional information
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enzyme deleltion strain, cells are viable only if supplemented with extracellular mannose and glucose. Increase of extracellular mannose concentration results in significantly reduced growth rates without alterations in intracellular GDP-mannose levels and in increase of mannose 6-phosphate levels
additional information
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inactivation of the manA gene encoding phosphomannose isomerase results in production of amphotericins and their aglycones, 8-deoxyamphoteronolides. A double mutant lacking the phosphomannose isomerase and phosphomannomutase genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins
