EC - D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphatase
Other names:
gmhB (gene name)
yaeD (gene name)
Systematic name:
D-glycero-β-D-manno-heptose 1,7-bisphosphate 7-phosphohydrolase



The enzyme is involved in biosynthesis of ADP-L-glycero-β-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core in Gram-negative bacteria. In vitro the catalytic efficiency with the β-anomer is 100-200-fold higher than with the α-anomer [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (21) [show] [UniProt]


  1. Kneidinger, B., Marolda, C., Graninger, M., Zamyatina, A., McArthur, F., Kosma, P., Valvano, M. A., Messner, P.
    Biosynthesis pathway of ADP-L-glycero-β-D-manno-heptose in Escherichia coli.
    J. Bacteriol. 184: 363-369 (2002). [PMID: 11751812]
  2. Valvano, M. A., Messner, P., Kosma, P.
    Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides.
    Microbiology 148: 1979-1989 (2002). [PMID: 12101286]
  3. Wang, L., Huang, H., Nguyen, H. H., Allen, K. N., Mariano, P. S., Dunaway-Mariano, D.
    Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).
    Biochemistry 49: 1072-1081 (2010). [PMID: 20050615]

[EC created 2010]