INVOLVEMENT OF ARGININE RESIDUES IN THE CATALYTIC ACTIVITY OF CATECHOL-O-METHYLTRANSFERASE

被引:2
作者
TUNNICLIFF, G [1 ]
NGO, TT [1 ]
机构
[1] CLIN RES INST MONTREAL, MONTREAL H2W 1R7, QUEBEC, CANADA
来源
GENERAL PHARMACOLOGY-THE VASCULAR SYSTEM | 1979年 / 10卷 / 05期
关键词
D O I
10.1016/0306-3623(79)90073-9
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
1. 1. Phenylglyoxal, a specific chemical modifier of arginine residues, rapidly inactivated brain and liver catechol-O-methyltransferase (COMT) of rat. 2. 2. The inactivation was first order dependent, and the rate was calculated as 0.71 min-7 and 0.67 min-1 at pH 7.8 and 23°C for the brain and liver enzyme respectively. 3. 3. The presence of the substrate S-adenosyl-methionine during the preincubation of COMT with the phenyl-glyoxal markedly reduced the rate of inactivation. 4. 4. Three other dicarbonyl compounds 2,4-pentanedione, 2,3-butanedione and 1,2-cyclohexanedione also inactivated the enzyme. 5. 5. The results suggest that arginine residues play an important role in the catalytic activity of rat brain and liver COMT. © 1979.
引用
收藏
页码:373 / 376
页数:4
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