SPECIFICITY OF GUINEA-PIG LIVER TRANSGLUTAMINASE FOR AMINE SUBSTRATES

被引：123

作者：

LORAND, L ^{[1
]}

PARAMESWARAN, KN ^{[1
]}

STENBERG, P ^{[1
]}

TONG, YS ^{[1
]}

VELASCO, PT ^{[1
]}

JONSSON, NA ^{[1
]}

MIKIVER, L ^{[1
]}

MOSES, P ^{[1
]}

机构：

[1] KABI AB,DEPT ORGAN CHEM,S-11287 STOCKHOLM,SWEDEN

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 09期

关键词：

D O I：

10.1021/bi00576a019

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 amine specificity of guinea pig liver transglutaminase, a model enzyme for endo-Y-glutamine:e-lysine transferases, was explored with the aid of synthetic substrates of high apparent affinities. As exemplified by dansyl- (5-dimethylamino-l-naphthalenesulfonyl), (2,4-dinitroben-zenesulfonyl)-, and (2,4,6-triisopropylbenzenesulfonyl)-cadaverines—each of which showed affinities of approximately 4 × 107 M-1—the best amine substrates carried a large hy-drophobic substituent attached to an alkylamine side chain of about 7.2 υ in length. Altogether, our results point to the importance of a hydrophobic binding region in the enzyme from where the alkyl side chain reaches into a narrow crevice toward the active center and positions the primary amine of the substrate for attacking the carbonyl group of the acyl enzyme intermediate. © 1979, American Chemical Society. All rights reserved.

引用

页码：1756 / 1765

页数：10

共 50 条

[1]

ABERNETHY JL, 1977, J BIOL CHEM, V252, P1837

[2] ISOPEPTIDE CROSSLINKS - THEIR OCCURRENCE AND IMPORTANCE IN PROTEIN STRUCTURE [J].