BACTERIAL ADENYLYL CYCLASES

被引：43

作者：

PETERKOFSKY, A ^{[1
]}

REIZER, A ^{[1
]}

REIZER, J ^{[1
]}

GOLLOP, N ^{[1
]}

ZHU, PP ^{[1
]}

AMIN, N ^{[1
]}

机构：

[1] UNIV CALIF SAN DIEGO,DEPT BIOL,LA JOLLA,CA 92093

来源：

PROGRESS IN NUCLEIC ACID RESEARCH AND MOLECULAR BIOLOGY, VOL 44 | 1993年 / 44卷

关键词：

D O I：

10.1016/S0079-6603(08)60216-0

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：

This chapter describes the enzyme (adenylyl cyclase) that effect the synthesis of Adenosine 3’,5’-cyclic monophosphate (cAMP) in various bacterial species. The content will rather reflect current major interests. The adenylyl cyclase from Escherichia coli has been a major subject of research interest ever since it was identified as the probable point for physiological regulation of cAMP levels in that organism and therefore a prime candidate for a protein mediator of the catabolite repression response mechanism. cAMP functions as a cytoplasmic element mediating some reactions crucial for efficient cellular function. An activity that has been found only in eukaryotic cells is the CAMP-dependent protein kinase. This enzyme is a well-known target of the action of cAMP as a second messenger, in which action this ligand transmits a signal generated by an extracellular hormone. The manner in which cAMP acts on the cAMP-dependent protein kinase involves a release of the catalytic moiety of the enzyme from a complex in which its activity is inhibited as a result of binding to a regulatory subunit. © 1993 Academic Press Inc.

引用

页码：31 / 65

页数：35

共 116 条

[1] THE COMPLETE NUCLEOTIDE-SEQUENCE OF THE ADENYLATE-CYCLASE GENE OF ESCHERICHIA-COLI [J].