LmbB2 – a unique tyrosine hydroxylase operating in lincomycin

Number of the records: 1

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SYSNO ASEP	0320605
Document Type	A - Abstract
R&D Document Type	The record was not marked in the RIV
R&D Document Type	Není vybrán druh dokumentu
Title	LmbB2 – a unique tyrosine hydroxylase operating in lincomycin
Title	LmbB2 – unikátní hydroxylaáza tyrosinu operujici v biosyntéze linkomycinu
Author(s)	Novotná, Jitka (MBU-M) Olšovská, Jana (MBU-M) Mojzes, P. (CZ) Novák, Petr (MBU-M)_{RID, ORCID} Marečková, M. (CZ) Janata, Jiří (MBU-M)_{RID, ORCID} Spížek, Jaroslav (MBU-M)
Source Title	Trends in Enzymology 2008. - St. Malo : Elsevier, 2008 S. 67-67
Number of pages	1 s.
Action	Trends in Enzymology 2008
Event date	02.07.2008-05.07.2008
VEvent location	St. Malo
Country	FR - France
Event type	WRD
Language	eng - English
Country	FR - France
Keywords	lincomycin
Subject RIV	EE - Microbiology, Virology
R&D Projects	IAA500200810 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
CEZ	AV0Z50200510 - MBU-M (2005-2011)
Annotation	Lincomycin A and its derivatives are potent antibiotics showing antibacterial and some of them also antimalarial activity. Structurally, lincomycin A is composed of two amide bonded subunits, methylthiolincosamide and methylpropylproline. The pathway leading from tyrosine to propylproline was proposed based on determination of the biosynthetic origin of the carbon and nitrogen atoms1
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2009

Number of the records: 1