NOVOTNÁ, Jitka, Jana OLSOVSKA, Petr NOVAK, Peter MOJZEŠ, Radka CHALOUPKOVÁ, Zdenek KAMENIK, Jaroslav SPIZEK, Eva KUTEJOVA, Markéta MAREČKOVÁ, Pavel TICHY, Jiří DAMBORSKÝ and Jiri JANATA. Lincomycin Biosynthesis Involves a Tyrosine Hydroxylating Heme Protein of an Unusual Enzyme Family. Plos One. SAN FRANCISCO: PUBLIC LIBRARY SCIENCE, 2013, vol. 8, No 12, p. "e79974-1"-"e79974-10", 10 pp. ISSN 1932-6203. doi:10.1371/journal.pone.0079974.
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Basic information
Original name Lincomycin Biosynthesis Involves a Tyrosine Hydroxylating Heme Protein of an Unusual Enzyme Family
Authors NOVOTNÁ, Jitka (203 Czech Republic, guarantor, belonging to the institution), Jana OLSOVSKA (203 Czech Republic), Petr NOVAK (203 Czech Republic), Peter MOJZEŠ (203 Czech Republic), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Zdenek KAMENIK (203 Czech Republic), Jaroslav SPIZEK (203 Czech Republic), Eva KUTEJOVA (203 Czech Republic), Markéta MAREČKOVÁ (203 Czech Republic), Pavel TICHY (203 Czech Republic), Jiří DAMBORSKÝ (203 Czech Republic, belonging to the institution) and Jiri JANATA (203 Czech Republic).
Edition Plos One, SAN FRANCISCO, PUBLIC LIBRARY SCIENCE, 2013, 1932-6203.
Other information
Original language English
Type of outcome Article in a journal
Field of Study Biotechnology and bionics
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.534
RIV identification code RIV/00216224:14740/13:00072277
Organization unit Central European Institute of Technology
UT WoS 000327949300014
Tags ok, rivok
Tags International impact, Reviewed
Changed by Changed by: Olga Křížová, učo 56639. Changed: 8. 4. 2014 02:15.
The gene lmbB2 of the lincomycin biosynthetic gene cluster of Streptomyces lincolnensis ATCC 25466 was shown to code for an unusual tyrosine hydroxylating enzyme involved in the biosynthetic pathway of this clinically important antibiotic. LmbB2 was expressed in Escherichia coli, purified near to homogeneity and shown to convert tyrosine to 3,4-dihydroxyphenylalanine (DOPA). In contrast to the well-known tyrosine hydroxylases (EC and tyrosinases (EC, LmbB2 was identified as a heme protein. Mass spectrometry and Soret band-excited Raman spectroscopy of LmbB2 showed that LmbB2 contains heme b as prosthetic group. The CO-reduced differential absorption spectra of LmbB2 showed that the coordination of Fe was different from that of cytochrome P450 enzymes. LmbB2 exhibits sequence similarity to Orf13 of the anthramycin biosynthetic gene cluster, which has recently been classified as a heme peroxidase. Tyrosine hydroxylating activity of LmbB2 yielding DOPA in the presence of (6R)-5,6,7,8-tetrahydro-L-biopterin (BH4) was also observed. Reaction mechanism of this unique heme peroxidases family is discussed. Also, tyrosine hydroxylation was confirmed as the first step of the amino acid branch of the lincomycin biosynthesis.
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
LC06010, research and development projectName: Centrum biokatalýzy a biotransformací
Investor: Ministry of Education, Youth and Sports of the CR, Center of Biocatalysis and Biotransformation
MSM0021622412, plan (intention)Name: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Acronym: INCHEMBIOL)
Investor: Ministry of Education, Youth and Sports of the CR, Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL)
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