Substrate scope for trimethyllysine hydroxylase catalysis

被引：17

作者：

Al Temimi, Abbas H. K. ^{[1
]}

Pieters, Bas J. G. E. ^{[1
]}

Reddy, Y. Vijayendar ^{[1
]}

White, Paul B. ^{[1
]}

Mecinovic, Jasmin ^{[1
]}

机构：

[1] Radboud Univ Nijmegen, Inst Mol & Mat, Heyendaalseweg 135, NL-6525 AJ Nijmegen, Netherlands

来源：

CHEMICAL COMMUNICATIONS | 2016年 / 52卷 / 87期

关键词：

GAMMA-BUTYROBETAINE HYDROXYLASE; EPSILON-N-TRIMETHYLLYSINE; CARNITINE BIOSYNTHESIS; 3-HYDROXY-N6-TRIMETHYL-LYSINE; N6-TRIMETHYL-LYSINE; METABOLISM;

D O I：

10.1039/c6cc07845a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Trimethyllysine hydroxylase (TMLH) is a non-haem Fe(II) and 2-oxoglutarate dependent oxygenase that catalyses the C-3 hydroxylation of an unactivated C-H bond in L-trimethyllysine in the first step of carnitine biosynthesis. The examination of trimethyllysine analogues as substrates for human TMLH reveals that the enzyme does hydroxylate substrates other than natural L-trimethyllysine.

引用

页码：12849 / 12852

页数：4

共 24 条

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