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
-
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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Crystallization
Crystallization on EC 5.3.1.8 - mannose-6-phosphate isomerase
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structure complexed with inhibitor 5-phospho-D-arabinonhydrazide at 1.85 A resolution. Glu294 is the catalytic base that transfers a proton between the C1 and C2 carbon atoms of the substrate. The inhibitor shows bidentate coordination
homology modeling of structure and refinement by energy minimization and molecular dynamics
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both in complex with fructose 6-phosphate and with glucose 6-phosphate
enzyme in apoform without metal ion, in the holoform with bound Zn2+, or complexed with bound inhibitor yttrium, or with Zn2+ and fructose 6-phosphate, microbatch method, 0.003 ml of protein solution and crystallization solution are mixed containing 4 mg/ml protein, 0.1 M magnesium acetate, 0.2 M sodium cacodylate, pH 6.5, 20% PEG 8000 and 5% dioxane, addition of 10 mM metal ions and 250 mM fructose 6-phosphate for complexed enzyme, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement
to 1.66 A resolution, space group P212121. Preliminary structure solution by molecular replacement using the strucutre from Candida albicans mannose-6-phosphate isomerase
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