Biosynthesis of sialic acids by Neisseria meningitidis.
نویسندگان
چکیده
Recent reports from this laboratory (2-4) and other laboratories (5, 6) have elucidated the pathway of biosynthesis of N-acetylneuraminic acid from N-acetyl-n-mannosamine and phosphoenolpyruvic acid in mammalian systems. The over-all biosynthetic reaction for rat liver and bovine submaxillary gland is catalyzed by 3 enzymes: a kinase, a condensing enzyme, and a dephosphorylating enzyme. N-Acetyl-n-mannosamine is phosphorylated by a specific kinase and adenosine triphosphate to yield N-acetyl-n-mannosamine 6phosphate. This condenses with phosphoenolpyruvic acid to give N-acetylneuraminic acid 9-phosphati according to Equation 1.
منابع مشابه
The siaA gene involved in capsule polysaccharide biosynthesis of Neisseria meningitidis B codes for N-acylglucosamine-6-phosphate 2-epimerase activity.
The capsule polysaccharide of Neisseria meningitidis serogroup B is composed of a homopolymer of alpha-2-->8 linked N-acetyl-neuraminic acid (sialic acid). The enzymes required for sialic acid biosynthesis and polymerization are encoded in region A of the capsule gene complex. We here describe the enzymatic activity of the siaA gene product as determined by biochemical analysis. siaA was overex...
متن کاملThe sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease
Glycomics is a rapidly growing field that focuses on the structure and function of carbohydrates (glycans) in biological systems. Glycan interactions play a major role in infectious disease, at all stages of colonisation and disease progression. Neisseria meningitidis, the cause of meningococcal sepsis and meningitis, and Neisseria gonorrhoeae, which causes the sexually transmitted infection go...
متن کاملStructure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP.
The x-ray crystallographic structure of selenomethionyl cytosine-5'-monophosphate-acylneuraminate synthetase (CMP-NeuAc synthetase) from Neisseria meningitidis has been determined at 2.0-A resolution using multiple-wavelength anomalous dispersion phasing, and a second structure, in the presence of the substrate analogue CDP, has been determined at 2.2-A resolution by molecular replacement. This...
متن کاملNonopsonic phagocytosis of group C Neisseria meningitidis by human neutrophils.
Although complement-mediated bactericidal activity in serum has long been known to be very important in host defense against Neisseria meningitidis, recent studies have shown that opsonic phagocytosis by neutrophils is also important. The purpose of this study was to determine if endemic group C N. meningitidis strains were susceptible to nonopsonic (complement- and antibody-independent) phagoc...
متن کاملSuccessive glycosyltransfer of sialic acid by Escherichia coli K92 polysialyltransferase in elongation of oligosialic acceptors.
Escherichia coli K92 produces a capsular polysialic acid with alternating alpha2,8 alpha2,9 NeuNAc linkages. This polysaccharide is cross-reactive with the neuroinvasive pathogen Neisseria meningitidis Group C. The K92 polysialyltransferase (PST) catalyzes the synthesis of the polysialic acid with alternating linkages by the transfer of NeuNAc from CMP-NeuNAc to the nonreducing end of the growi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 237 شماره
صفحات -
تاریخ انتشار 1962