Literature DB >> 3586666

Resolution and reconstitution of cytochrome P-450 containing steroid hydroxylation system of Rhizopus nigricans.

K Breskvar, B Cresnar, T Hudnik-Plevnik.   

Abstract

11 alpha-hydroxylation of progesterone in the eucaryotic filamentous fungus Rhizopus nigricans is catalyzed by a monooxygenase. Three components of this multienzyme system, cytochrome P-450, rhizoporedoxin and a FAD containing rhizoporedoxin reductase have been separated from the postmitochondrial fraction on DEAE cellulose. Using NADPH as electron donor we showed that the presence of all three components was necessary for the reconstitution of the active electron transport chain.

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Year:  1987        PMID: 3586666     DOI: 10.1016/0022-4731(87)90063-x

Source DB:  PubMed          Journal:  J Steroid Biochem        ISSN: 0022-4731            Impact factor:   4.292


  1 in total

1.  Characterization and Solubilization of Kaurenoic Acid Hydroxylase from Gibberella fujikuroi.

Authors:  J. C. Jennings; R. C. Coolbaugh; D. A. Nakata; C. A. West
Journal:  Plant Physiol       Date:  1993-03       Impact factor: 8.340

  1 in total

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