Characterization of glycine N-methyltransferase from rabbit liver

被引:8
|
作者
Kloor, D
Karnahl, K
Kömpf, J
机构
[1] Univ Tubingen, Fac Med, Dept Pharmacol & Toxicol, D-72074 Tubingen, Germany
[2] Univ Tubingen, Fac Med, Inst Anthropol & Human Genet, D-72074 Tubingen, Germany
关键词
glycine N-methyltransferase; S-adenosylhomocysteine; S-adenosylmethionine; sarcosine oxidase; peroxidase;
D O I
10.1139/O04-007
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 enzymatic properties of glycine N-methyltransferase from rabbit liver and the effects of endogenous adenosine nucleosides, nucleotides and methyltransferase inhibitors were investigated using a photometrical assay to detect sarcosine with o-dianisidine as a dye. After isolation and purification the denatured enzyme showed a two-banded pattern by SDS-PAGE. The enzyme was highly specific for its substrates with a pH-optimum at pH 8.6. Glycine N-methyltransferase exhibits Michaelis-Menten kinetics for its substrates, S-adenosylmethionine and glycine, respectively. The apparent K-m and V-max values were determined for both the substrates, the other substrate being present at saturating concentrations. The enzyme was strongly inhibited in the presence of S-adenosylhomocysteine, 3-deazaadenosine, and 5'-S-isobutylthio-5'-deoxyadenosine. All other inhibitors investigated, adenosine, 2'-deoxyadenosine, aciclovir, and 5'-N-ethylcarboxamidoadenosine were poor inhibitors of the methylation rection. Adenine nucleotides and vidarabin were without effect on the enzymatic activity. Based on the kinetic data glycine N-methyltransferase from rabbit liver exhibits appreciable activity at physiological S-adenosylmethionine and S-adenosylhomocysteine levels.
引用
收藏
页码:369 / 374
页数:6
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