Úvodní kroky v biosynthése lincomycinu

Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F05%3A00023838" target="_blank" >RIV/61388971:_____/05:00023838 - isvavai.cz</a>
Výsledek na webu
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DOI - Digital Object Identifier
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Jazyk výsledku
angličtina
Název v původním jazyce
The initial steps in lincomycin biosynthesis
Popis výsledku v původním jazyce
Protein LmbB1, involved in lincomycin biosynthesis in Streptomyces lincolnensis, was expressed in Escherichia coli and purified in its active form. It was found that it is a dimer consisting of identical subunits. By means of capillary electrophoresis and mass spectrometry, chemical structure of the reaction product of this protein was determined. LmbB1 was identified as dioxygenase catalyzing 2,3-extradiol splitting of L-3,4-dihydroxyphenylalanine (DOPA) aromatic ring. Protein LmbB2 was also expressedin E. coli and purified in its active form. It was identified as monooxidase catalyzing hydroxylation of tyrosine to DOPA
Název v anglickém jazyce
The initial steps in lincomycin biosynthesis
Popis výsledku anglicky
Protein LmbB1, involved in lincomycin biosynthesis in Streptomyces lincolnensis, was expressed in Escherichia coli and purified in its active form. It was found that it is a dimer consisting of identical subunits. By means of capillary electrophoresis and mass spectrometry, chemical structure of the reaction product of this protein was determined. LmbB1 was identified as dioxygenase catalyzing 2,3-extradiol splitting of L-3,4-dihydroxyphenylalanine (DOPA) aromatic ring. Protein LmbB2 was also expressedin E. coli and purified in its active form. It was identified as monooxidase catalyzing hydroxylation of tyrosine to DOPA

Rok uplatnění
2005
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Podobné výsledky(10)