BINDING OF N-CARBOXYMETHYL DIPEPTIDE INHIBITORS TO THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY - A NOVEL CLASS OF TRANSITION-STATE ANALOGS FOR ZINC PEPTIDASES

被引：168

作者：

MONZINGO, AF

MATTHEWS, BW

机构：

[1] UNIV OREGON,INST MOLEC BIOL,EUGENE,OR 97403

[2] UNIV OREGON,DEPT PHYS,EUGENE,OR 97403

来源：

BIOCHEMISTRY | 1984年 / 23卷 / 24期

关键词：

D O I：

10.1021/bi00319a010

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：

引用

页码：5724 / 5729

页数：6

共 32 条

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[2] BOLOGNESI MC, 1979, J BIOL CHEM, V254, P634
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[7] AN INTERACTIVE COMPUTER-GRAPHICS STUDY OF THERMOLYSIN-CATALYZED PEPTIDE CLEAVAGE AND INHIBITION BY N-CARBOXYMETHYL DIPEPTIDES
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[8] BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN CATALYSIS
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[J]. BIOCHEMISTRY, 1981, 20 (24) : 6912 - 6920
[9] STRUCTURE OF THERMOLYSIN REFINED AT 1.6-A RESOLUTION
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[J]. JOURNAL OF MOLECULAR BIOLOGY, 1982, 160 (04) : 623 - 639
[10] METAL-COORDINATING SUBSTRATE-ANALOGS AS INHIBITORS OF METALLOENZYMES
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[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (12) : 6216 - 6220

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