STABILIZATION OF THE OXY FORM OF TYROSINASE BY A SINGLE CONSERVATIVE AMINO-ACID SUBSTITUTION

被引：20

作者：

JACKMAN, MP ^{[1
]}

HUBER, M ^{[1
]}

HAJNAL, A ^{[1
]}

LERCH, K ^{[1
]}

机构：

[1] UNIV ZURICH,INST BIOCHEM,CH-8057 ZURICH,SWITZERLAND

来源：

BIOCHEMICAL JOURNAL | 1992年 / 282卷

关键词：

D O I：

10.1042/bj2820915

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Asp-208 of Streptomyces glaucescens tyrosinase (an invariant residue in the Cu(B)-binding region of tyrosinases and haemocyanins) was conservatively substituted by glutamic acid. Although having little effect on spectroscopic or kinetic properties of the enzyme, the mutation greatly decreased the lability of Cu-bound O2. A rationalization for these results is given, based on the crystal structure of Panulirus interruptus haemocyanin in the conserved Cu(B)-binding region.

引用

页码：915 / 918

页数：4