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Characterization of CJ1293, a new UDP‐GlcNAc C 6 dehydratase from Campylobacter jejuni 1
Author(s) -
Creuzenet Carole
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00057-2
Subject(s) - campylobacter jejuni , dehydratase , biochemistry , glycosylation , enzyme , cofactor , chemistry , biosynthesis , nucleotide sugar , acyl carrier protein , nad+ kinase , biology , bacteria , genetics
Campylobacter jejuni encodes numerous sugar‐nucleotide‐modifying enzymes potentially involved in the biosynthesis of surface carbohydrates. One of them, CJ1293, is involved in flagellin glycosylation but its biochemical activity remains unknown. Using over‐expressed and purified protein, we demonstrate that CJ1293 has UDP‐GlcNAc‐specific C 6 dehydratase activity. Catalysis occurs without addition of cofactor, suggesting internal recycling of NAD(P) + . The K m for UDP‐GlcNAc of 50 μM indicates that CJ1293 has higher affinity for its substrate than previously characterized homologues. Based on enzymatic data, we propose that CJ1293 catalyzes the first step in the biosynthesis of bacillosamine, a sugar found in C. jejuni 's protein glycosylation motifs.