Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Catherine L. Drennan"'
Publikováno v:
Nature
Oxetanocin A (OXT-A) is a potent antitumour, antiviral and antibacterial compound. Biosynthesis of OXT-A has been linked to a plasmid-borne Bacillus megaterium gene cluster that contains four genes: oxsA, oxsB, oxrA and oxrB. Here we show that both t
Autor:
Tzanko Doukov, Nozomi Ando, Catherine L. Drennan, Stephen W. Ragsdale, Javier Seravalli, Güneş Bender, Yan Kung, Leah C. Blasiak
Publikováno v:
Nature
The first three-dimensional description of all the protein modules required for the activation, protection and catalytic steps of B12-dependent methyl transfer. Vitamin B12 (cobalamin) and its derivatives are important cofactors in a broad range of b
Autor:
Jésus Fernández-Zapata, Subramanian Padmanabhan, Juan Manuel Ortiz-Guerrero, Percival Yang-Ting Chen, Gyunghoon Kang, María Carmen Polanco, Marco Jost, Catherine L. Drennan, Montserrat Elías-Arnanz
Publikováno v:
Nature
PMC
Digital.CSIC. Repositorio Institucional del CSIC
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PMC
Digital.CSIC. Repositorio Institucional del CSIC
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Photoreceptor proteins enable organisms to sense and respond to light. The newly discovered CarH-type photoreceptors use a Vitamin B derivative, adenosylcobalamin, as the light-sensing chromophore to mediate light-dependent gene regulation. Here we p
Publikováno v:
Nature. 437:838-844
The biosynthetic pathway of the clinically important antibiotic fosfomycin uses enzymes that catalyse reactions without precedent in biology. Among these is hydroxypropylphosphonic acid epoxidase, which represents a new subfamily of non-haem mononucl
Autor:
Catherine L. Drennan, Steven O. Mansoorabadi, Wei-Chen Chang, Mishtu Dey, Pinghua Liu, Zongbao K. Zhao, Hung-wen Liu, Sung-Ju Moon
Publikováno v:
Nature
The non-haem-iron-dependent enzyme HppE catalyses the final step in the biosynthesis of fosfomycin, a broad-spectrum, clinically useful antibiotic; here it is shown that HppE can also catalyse a 1,2-phosphono-migration reaction, previously undocument
Publikováno v:
Nature. 440(7082)
Non-haem Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzymes harness the reducing power of alphaKG to catalyse oxidative reactions, usually the hydroxylation of unactivated carbons, and are involved in processes such as natural product biosynthesi