Zobrazeno 1 - 5
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pro vyhledávání: '"Jenna K. Capyk"'
Autor:
Lindsay D. Eltis, Israël Casabon, Natalie C. J. Strynadka, Robert J. Gruninger, Jenna K. Capyk
Publikováno v:
Journal of Biological Chemistry. 286:40717-40724
Mycobacterium tuberculosis (Mtb), a significant global pathogen, contains a cholesterol catabolic pathway. Although the precise role of cholesterol catabolism in Mtb remains unclear, the Rieske monooxygenase in this pathway, 3-ketosteroid 9α-hydroxy
Autor:
Rainer Kalscheuer, Hyukin Kwon, Jie Liu, Gordon R. Stewart, William W. Mohn, Sachi Okamoto, Rafael Zhao, Jenna K. Capyk, Lindsay D. Eltis, William R. Jacobs
Publikováno v:
Journal of Biological Chemistry. 284:35534-35542
Cyp125 (Rv3545c), a cytochrome P450, is encoded as part of the cholesterol degradation gene cluster conserved among members of the Mycobacterium tuberculosis complex. This enzyme has been implicated in mycobacterial pathogenesis, and a homologue init
Publikováno v:
Journal of Biological Chemistry. 284:9937-9946
KshAB (3-Ketosteroid 9α-hydroxylase) is a two-component Rieske oxygenase (RO) in the cholesterol catabolic pathway of Mycobacterium tuberculosis. Although the enzyme has been implicated in pathogenesis, it has largely been characterized by bioinform
Autor:
Lindsay D. Eltis, Jenna K. Capyk
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 17(3)
As metalloenzymes capable of transforming a broad range of substrates with high stereo- and regio-specificity, the multicomponent Rieske oxygenases (ROs) have been studied in bacterial systems for applications in bioremediation and industrial biocata
Publikováno v:
Encyclopedia of Inorganic and Bioinorganic Chemistry
KshAB is a Rieske oxygenase (RO) in the aerobic steroid degradation pathways of bacteria. It is a monooxygenase responsible for the 9α-hydroxylation of the nucleus of 3-keto-4-ene steroids bearing short side chains at C17. It is composed of two doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5fb315ee42217580a51d66f44d96dc2
https://doi.org/10.1002/0470028637.met280
https://doi.org/10.1002/0470028637.met280