Tzeng YL, Datta A, Strole CA, Birck MR, Taylor WP, Carlson RW, Woodard RW, Stephens DS KpsF is the arabinose 5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid (Kdo) biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression in Neisseria meningitidis Journal of Biological Chemistry277(27) (2002)
24103-24113
NCBI PubMed ID:11956197 Journal NLM ID:2985121R Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology Institutions: Division of Infectious Diseases, Department of Medicine, Emory University School of Medicine, Atlanta, GA 30303
We have identified and defined the function of kpsF of Neisseria meningitidis, and the homologues of kpsF in encapsulated K1 and K5 Escherichia coli. KpsF was shown to be the arabinose 5-phosphate isomerase, an enzyme not previously identified in prokaryotes that mediates the interconversion of ribulose 5-phosphate and arabinose 5- phosphate. KpsF is required for 3-deoxy-D-manno-octulosonic acid (Kdo) biosynthesis in N. meningitidis. Mutation of kpsF or the gene encoding the CMP-Kdo synthetase (kpsU/kdsB) in N. meningitidis resulted in expression of a lipooligossaccharide (LOS) structure that contained only lipid A and reduced capsule expression in the five invasive disease associated meningococcal serogroups (A, B, C, Y, and W-135). The step linking meningococcal capsule and LOS biosynthesis was shown to be Kdo production as the expression of capsule was wild type in a Kdo transferase (kdtA) mutant. Thus, in addition to lipooligosaccharide assembly, Kdo is required for meningococcal capsular polysaccharide expression. Further, N. meningitidis, unlike enteric gram-negative bacteria, can survive and synthesize only unglycosylated lipid A
Methods: biochemical methods Biosynthesis and genetic data: biosynthesis data
Related record ID(s): 5408, 5409 NCBI Taxonomy refs (TaxIDs):562 Reference(s) to other database(s): GTC:G70705ZI, GlycomeDB:37103 Show glycosyltransferases
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