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LmbB2 – a unique tyrosine hydroxylase operating in lincomycin
- 1.
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. 67-67Number 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