兔肝提取物催化的核糖核酸酶A的糖基化作用。
Glycosylation of ribonuclease A catalysed by rabbit liver extracts.
作者信息
Khalkhall Z, Marshall R D
出版信息
Biochem J. 1975 Feb;146(2):299-307. doi: 10.1042/bj1460299.
Abstract
Crude extracts of rabbit liver catalyse in vitro the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to bovine pancreatic ribonuclease A. The enzymic activity is contained in rough endoplasmic reticulum. It has an absolute requirement for a bivalent metal ion: Co-2+ greater than Mn-2+ greater than Ni-2+. Mg-2+ is ineffective. There is enzymic activity in the absence of detergent, but increased activity is observed in the presence of Triton X-100. The site of glycosylation of ribonuclease A is asparagine-34, and glycosylation occurs only at this point. These findings agree with the hypothesis that the sequence Asn-X-Thr(Ser) (where X may be one of a number of types of amino acid) is a necessary, but not sufficient, condition for N-acetylglucosaminylation of a protein-bound asparagine residue.
摘要
兔肝粗提物在体外催化N-乙酰葡糖胺从UDP-N-乙酰葡糖胺转移至牛胰核糖核酸酶A。酶活性存在于糙面内质网中。它对二价金属离子有绝对需求：Co²⁺＞Mn²⁺＞Ni²⁺。Mg²⁺无效。在没有去污剂的情况下存在酶活性，但在Triton X-100存在时观察到活性增加。核糖核酸酶A的糖基化位点是天冬酰胺-34，且糖基化仅在此位点发生。这些发现与以下假说相符，即序列Asn-X-Thr（Ser）（其中X可能是多种氨基酸类型之一）是蛋白质结合的天冬酰胺残基进行N-乙酰葡糖胺化的必要但不充分条件。
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