ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES

被引：105

作者：

GAMBLIN, SJ ^{[1
]}

DAVIES, GJ ^{[1
]}

GRIMES, JM ^{[1
]}

JACKSON, RM ^{[1
]}

LITTLECHILD, JA ^{[1
]}

WATSON, HC ^{[1
]}

机构：

[1] UNIV BRISTOL,SCH MED SCI,DEPT BIOCHEM,BRISTOL BS8 1TD,AVON,ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 219卷 / 04期

关键词：

TYPE-I ALDOLASE; TERTIARY STRUCTURE; ENZYME MECHANISM; POINT MUTATIONS; PARASITIC DISEASES;

D O I：

10.1016/0022-2836(91)90650-U

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：

The structure of the type I fructose 1,6-bisphosphate aldolase from human muscle has been extended from 3 Å to 2 Å resolution. The improvement in the resulting electron density map is such that the 20 or so C-terminal residues, known to be associated with activity and isozyme specificity, have been located. The side-chain of the Schiff's base-forming lysine 229 is located towards the centre of an eight-stranded β-barrel type structure. The C-terminal "tail" extends from the rim of the β-barrel towards lysine 229, thus forming part of the active site of the enzyme. This structural arrangement appears to explain the difference in activity and specificity of the three tissue-specific human aldolases and helps with our understanding of the type I aldolase reaction mechanism. © 1991.

引用

页码：573 / 576

页数：4

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