| Entry |
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| Name |
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate 7-phosphatase;
gmhB (gene name)
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| Class |
Hydrolases;
Acting on ester bonds;
Phosphoric-monoester hydrolases
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| Sysname |
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase
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| Reaction(IUBMB) |
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-alpha-D-manno-heptose 1-phosphate + phosphate [RN: R09771]
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| Reaction(KEGG) |
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| Substrate |
D-glycero-alpha-D-manno-heptose 1,7-bisphosphate [CPD: C19879];
H2O [CPD: C00001]
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| Product |
D-glycero-alpha-D-manno-heptose 1-phosphate [CPD: C19880];
phosphate [CPD: C00009]
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| Comment |
The enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein in some Gram-positive bacteria. The in vitro catalytic efficiency of the enzyme from Bacteroides thetaiotaomicron is 6-fold higher with the alpha-anomer than with the beta-anomer [1].
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| History |
EC 3.1.3.83 created 2010
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| Pathway |
| ec00540 | Lipopolysaccharide biosynthesis |
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| Orthology |
| K03273 | D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase |
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| Genes |
» show all
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| Reference |
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| Authors |
Wang L, Huang H, Nguyen HH, Allen KN, Mariano PS, Dunaway-Mariano D |
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| Title |
Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB). |
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| Journal |
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| Sequence |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 3.1.3.83 |
| ExPASy - ENZYME nomenclature database: | 3.1.3.83 |
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