ExplorEnz: EC 5.3.1.28

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5.3.1.28

Accepted name:

D-sedoheptulose-7-phosphate isomerase

Reaction:

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate

Other name(s):

sedoheptulose-7-phosphate isomerase; phosphoheptose isomerase; gmhA (gene name); lpcA (gene name)

Systematic name:

D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase

Comments:

In Gram-negative bacteria 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-positive bacteria the enzyme is involved in biosynthesis of GDP-D-glycero-α-D-manno-heptose, which is required for assembly of S-layer glycoprotein.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Kneidinger, B., Marolda, C., Graninger, M., Zamyatina, A., McArthur, F., Kosma, P., Valvano, M.A. and Messner, P. Biosynthesis pathway of ADP-L-glycero-β-D-manno-heptose in Escherichia coli. J. Bacteriol. 184 (2002) 363–369. [DOI] [PMID: 11751812]
2.	Kneidinger, B., Graninger, M., Puchberger, M., Kosma, P. and Messner, P. Biosynthesis of nucleotide-activated D-glycero-D-manno-heptose. J. Biol. Chem. 276 (2001) 20935–20944. [DOI] [PMID: 11279237]
3.	Valvano, M.A., Messner, P. and Kosma, P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides. Microbiology 148 (2002) 1979–1989. [DOI] [PMID: 12101286]
4.	Kim, M.S. and Shin, D.H. A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (2009) 1110–1112. [DOI] [PMID: 19923728]
5.	Taylor, P.L., Blakely, K.M., de Leon, G.P., Walker, J.R., McArthur, F., Evdokimova, E., Zhang, K., Valvano, M.A., Wright, G.D. and Junop, M.S. Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants. J. Biol. Chem. 283 (2008) 2835–2845. [DOI] [PMID: 18056714]

[EC 5.3.1.28 created 2010]