DUAL-SPECIFICITY PROTEIN-KINASES - WILL ANY HYDROXYL DO

被引:226
作者
LINDBERG, RA
QUINN, AM
HUNTER, T
机构
[1] SALK INST BIOL STUDIES, CTR BIOCOMP, SAN DIEGO, CA 92138 USA
[2] UNIV CALIF SAN DIEGO, DEPT BIOL, LA JOLLA, CA 92093 USA
关键词
D O I
10.1016/0968-0004(92)90248-8
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
Protein kinases are classified by the target amino acid in their substrates. Those protein kinases that phosphorylate hydroxyamino acids comprise two groups, the protein-tyrosine and protein-serine/threonine kinases, which, until recently, had been thought to be mutually exclusive. However, several new protein kinases have been discovered that, by the criterion of primary structure, would be classified as protein-serine/threonine kinases but which, surprisingly, are able to phosphorylate tyrosine residues. Even more surprising, there are reports of protein kinases that are capable of phosphorylating both tyrosine and serine/threonine residues. We review and discuss recent developments concerning these 'dual-specificity' protein kinases.
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页码:114 / 119
页数:6
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