Substrate scope for trimethyllysine hydroxylase catalysis

Autor:	Jasmin Mecinović, Abbas H. K. Al Temimi, Y. Vijayendar Reddy, Bas J. G. E. Pieters, Paul B. White
Rok vydání:	2016
Předmět:	Oxygenase Stereochemistry Synthetic Organic Chemistry 010402 general chemistry 01 natural sciences Catalysis Hydroxylation chemistry.chemical_compound Trimethyllysine hydroxylase Materials Chemistry GeneralLiterature_REFERENCE(e.g. dictionaries encyclopedias glossaries) chemistry.chemical_classification 010405 organic chemistry Metals and Alloys Substrate (chemistry) General Chemistry 0104 chemical sciences Surfaces Coatings and Films Electronic Optical and Magnetic Materials Enzyme chemistry Biochemistry Carnitine biosynthesis Ceramics and Composites Physical Organic Chemistry
Zdroj:	Chemical Communications, 52, 87, pp. 12849-12852 Chemical Communications, 52, 12849-12852
ISSN:	1359-7345
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2ea39e9304188009e199589f4edf01c https://hdl.handle.net/2066/161427 Zobrazit plný text záznamu