青蟹（锯缘青蟹）碱性磷酸酶的一个必需赖氨酸残基。

An essential lysine residue of green crab (Scylla Serrata) alkaline phosphatase.

作者信息

Chen Q X, Zhou H M

机构信息

Department of Biological Science and Biotechnology, Tsinghua University, Beijing, People's Republic of China.

出版信息

Biochem Mol Biol Int. 1998 Oct;46(2):225-31. doi: 10.1080/15216549800203732.

DOI:10.1080/15216549800203732

PMID:9801790

Abstract

The values of pKa (10.38) and Hion (10.92 Kcal/mol) have been determined for the ionizing groups controlling activity of green crab alkaline phosphatase. The results suggest that -NH2 of lysine residue responsible for the ionization with pKc = 10.38 and delta H(o)ion = 10.92 Kcal/mol is in the active site of the enzyme. Modification of lysine residues of the enzyme by an excess of 2,4,6-trinitrobenzenesulfonic acid leads to complete inactivation. The two results coincide with each other. Quantitative assessment of the data indicates that among the reactive -NH2 groups modified only one is essential for the activity of the enzyme.

摘要

已确定控制青蟹碱性磷酸酶活性的电离基团的pKa值（10.38）和Hion值（10.92千卡/摩尔）。结果表明，pKc = 10.38且δH（o）ion = 10.92千卡/摩尔的负责电离的赖氨酸残基的-NH2位于酶的活性位点。用过量的2,4,6-三硝基苯磺酸修饰该酶的赖氨酸残基会导致完全失活。这两个结果相互吻合。数据的定量评估表明，在被修饰的反应性-NH2基团中，只有一个对酶的活性至关重要。