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LmbB2 – a unique tyrosine hydroxylase operating in lincomycin
- 1.0320605 - MBÚ 2009 SIGLE FR eng A - Abstract
Novotná, Jitka - Olšovská, Jana - Mojzes, P. - Novák, Petr - Marečková, M. - Janata, Jiří - Spížek, Jaroslav
LmbB2 – a unique tyrosine hydroxylase operating in lincomycin.
[LmbB2 – unikátní hydroxylaáza tyrosinu operujici v biosyntéze linkomycinu.]
Trends in Enzymology 2008. St. Malo: Elsevier, 2008. s. 67-67.
[Trends in Enzymology 2008. 02.07.2008-05.07.2008, St. Malo]
R&D Projects: GA AV ČR IAA500200810
Institutional research plan: CEZ:AV0Z50200510
Keywords : lincomycin
Subject RIV: EE - Microbiology, Virology
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
Protein LmbB2, kódovaný genem linkomycinového biosyntetického shluku byl nadprodukován v E. coli, charakterizován a určen jako unikátní hydroxyláza tyrosinu, obsahující hem jako prostetickou skupinu
Permanent Link: http://hdl.handle.net/11104/0169425
Number of the records: 1