By Alton Meister
Advances in Enzymology and comparable parts of Molecular Biology is a seminal sequence within the box of biochemistry, supplying researchers entry to authoritative experiences of the newest discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unmatched view of the ancient improvement of enzymology. The sequence bargains researchers the most recent figuring out of enzymes, their mechanisms, reactions and evolution, roles in complicated organic approach, and their software in either the laboratory and undefined. every one quantity within the sequence positive factors contributions through prime pioneers and investigators within the box from worldwide. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of themes and lengthy historic pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition through any scientist drawn to the invention of an enzyme, its houses, and its applications.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 52
11. Survey of Glycosyltransferases by Type of Sugar Transferred A. SIALYLTRANSFERASES I. Number and Types of Siulyltrunsferases The immediate precursor of glycosidically bound sialic acid is the sugar nucleotide, CMP-sialic acid. With this donor substrate, sialyltransferases catalyze the formation of sialic acid glycosides by transglycosylation according to reaction 2: CMP-sialic acid t HO-acceptor+Sialyl-0-acceptor + CMP-H (2) As shown in Table I, five sialic acid linkages commonly occur in a wide variety of mammalian glycoconjugates--Siaa2+6Gal, Siaa2BGa1, Siacu2-t 6GalNAc, Siaa2+6GlcNAc, and Siaa24Sia-and there is a single recent report of a Siaa2+4Gal linkage (36) and of a Siaa2+4GlcNAc linkage (20).
3 I Siaa2,6Gal81,4GlcNAcBi, 2 M a n a I,3 \ 0 ,Mond1,4GlcNAcBl,4 \ \ GalBI,4 2 Manul, 6 ‘GlcNAcBI, Fucal,3 / F u c u I,6 0 0 II 0 Siau2,3GalB1,3 @ /GlcNAcB‘sAsn ‘~alNAca-O-Thr/Ser @ Siau 2,s’~ III Fucal,2 GolNAcul,3 @ @ ,GOlBI,3 \ @ \GalNAca-O-Thr/Ser Siau2,6’@ Ip P ~ G ~ c U A B ~ , ~ G ~ ~ N A C ~ S B ~ , ~ ) ~ - G ~ C U,A 4 XBy ~l B, I ~- OG- ~Ser ~ B I , ~ G ~ ~ B I PT G l c u l , 2 G a l S I - O - Hyl @ 26 @ @ O 27 G L Y COSY LTRANSFERASES 2. The actions of different glycosyltransferases in oligosaccharide biosynthesis.
Purification of Glycosyltransferases A. General Considerations B. Affinity Chromatographic Methods C. Stabilization of Glycosyltransferases during Purification and Storage D. Criteria of Purity VI. Concluding Remarks Acknowledgment References 97 108 113 113 113 116 121 122 126 132 133 134 138 141 144 144 145 154 156 157 158 158 1. Introduction The glycosyltransferases comprise a group of enzymes that catalyze the synthesis of specific glycosides by transfer of a monosaccharide from a glycosylnucleotide (nucleotide-sugar) donor substrate to an acceptor substrate as shown in reaction 1: Glycosylnucleotide t acceptor +.