空肠弯曲杆菌
生物化学
化学
庚糖
葡萄糖醛酸
生物合成
立体化学
磷酸二羟丙酮
酶
微生物学
细菌
多糖
生物
突变体
遗传学
基因
作者
A.S. Riegert,Tamari Narindoshvili,Adriana Coricello,Nigel G. J. Richards,Frank M. Raushel
出处
期刊:Biochemistry
[American Chemical Society]
日期:2021-09-10
卷期号:60 (37): 2836-2843
被引量:9
标识
DOI:10.1021/acs.biochem.1c00439
摘要
Campylobacter jejuni is a Gram-negative, pathogenic bacterium that causes campylobacteriosis, a form of gastroenteritis. C. jejuni is the most frequent cause of food-borne illness in the world, surpassing Salmonella and E. coli. Coating the surface of C. jejuni is a layer of sugar molecules known as the capsular polysaccharide that, in C. jejuni NCTC 11168, is composed of a repeating unit of d-glycero-l-gluco-heptose, d-glucuronic acid, d-N-acetyl-galactosamine, and d-ribose. The d-glucuronic acid moiety is further amidated with either serinol or ethanolamine. It is unknown how these modifications are synthesized and attached to the polysaccharide. Here, we report the catalytic activities of two previously uncharacterized, pyridoxal phosphate (PLP)-dependent enzymes, Cj1436 and Cj1437, from C. jejuni NCTC 11168. Using a combination of mass spectrometry and nuclear magnetic resonance, we determined that Cj1436 catalyzes the decarboxylation of l-serine phosphate to ethanolamine phosphate. Cj1437 was shown to catalyze the transamination of dihydroxyacetone phosphate to (S)-serinol phosphate in the presence of l-glutamate. The probable routes to the ultimate formation of the glucuronamide substructures in the capsular polysaccharides of C. jejuni are discussed.
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