Identification of constitutive and herbicide inducible cytochromes P-450 in Streptomyces griseolus

  title={Identification of constitutive and herbicide inducible cytochromes P-450 in Streptomyces griseolus},
  author={Daniel P. O'Keefe and James A. Romesser and Kenneth J. Leto},
  journal={Archives of Microbiology},
The elevated soluble cytochrome P-450 content of Streptomyces griseolus cells found after growth in the presence of sulfonylurea herbicides has been shown to be the result of the appearance of one predominant cytochrome P-450 form. This cytochrome P-450 is the major soluble protein found to increase in amount following herbicide treatment, and functions as part of a sulfometuron methyl hydroxylase system. A second minor inducible cytochrome P-450 has been observed only in cells grown in the… 
Isolation and characterization of Streptomyces griseolus deletion mutants affected in cytochrome P-450-mediated herbicide metabolism
An in vivo delineation of the roles of the two different cytochrome P-450 systems in herbicide metabolism by S. griseolus is delineated, yielding an analysis of sulfonylurea metabolism mediated by cytochromes P- 450SU2 in the absence of P -450SU1.
Caffeine-inducible enzyme activity in Pseudomonas putida ATCC 700097
The data demonstrate that caffeine is metabolized through a specific biphasic pathway driven by oxygen-demanding enzymes in sewage bacteria.
Enhanced Heterologous Expression of Two Streptomyces griseolus Cytochrome P450s and Streptomyces coelicolor Ferredoxin Reductase as Potentially Efficient Hydroxylation Catalysts
ABSTRACT The herbicide-inducible, soluble cytochrome P450s CYP105A1 and CYP105B1 and their adjacent ferredoxins, Fd1 and Fd2, of Streptomyces griseolus were expressed in Escherichia coli to high
CYP201A2, a cytochrome P450 from Rhodopseudomonas palustris, plays a key role in the biodegradation of tributyl phosphate
This study shows that this O2- and NADPH/FMNH2-dependent process was also catalyzed when TBP was incubated with membrane-associated proteins extracted from this strain, suggesting a key role for a cytochrome P450 in this process.
Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
The study of streptomycete P450s involved in the biosynthesis of natural products has revealed their diverse roles in nature, expanded their catalytic repertoire, created structural and mechanistic paradigms, and exposed their potential for biomedical and biotechnological applications.
Degradation pathways of chlorsulfuron and metsulfuron-methyl by a Pseudomonas fluorescens strain
The results suggest that microbiological and chemical degradation can follow different path- ways in which the cleavage of sulfonylurea bridge takes place, and chemical hydrolysis allowed to identify different compounds from those obtained with biodegradation.
CYP105—diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces
A review of the diverse biological functions of CYP105s and the biosynthetic/catabolic pathways they are associated with provides a rich source for further investigation into the functions these enzymes fulfil and the metabolic pathways they participate in, in the natural environment.
Optimisation of Cytochrome P450 BM3 Assisted by Consensus-Guided Evolution
This work added several mutations to the BM3 mutant R966D/W1046S that enhanced the turnover number achievable with the inexpensive cofactors NADH and NBAH, and demonstrated that reactions driven by NADH with the NTD6 mutant not only surpassed total product output achievable by wild-type BM3 with NADPH but also retained the ability to use this latter cofactor with greatertotal product output as well.
SulE, a Sulfonylurea Herbicide De-Esterification Esterase from Hansschlegelia zhihuaiae S113
SulE catalyzed the de-esterification of a variety of sulfonylurea herbicides that gave rise to the corresponding herbicidally inactive parent acid and exhibited the highest catalytic efficiency toward thifensulfuron-methyl.


Induction of cytochrome P-450-dependent sulfonylurea metabolism in Streptomyces griseolus.
Cytochrome P-450 Reductase and Cytochrome b5 in Cytochrome P-450 Catalysis
The most completely described P-450 system, which is not membrane-bound, is associated with camphor metabolism in P. putida, and the involvement of cytochrome b 5 as a possible component of this electron transport chain is discussed.
Induction of cytochrome P-450 in Streptomyces griseus by soybean flour.
Demethylation of Veratrole by Cytochrome P-450 in Streptomyces setonii.
  • J. Sutherland
  • Biology, Chemistry
    Applied and environmental microbiology
  • 1986
The results suggest that S. setonii produces a cytochrome P-450 that is involved in the demethylation of veratrole and guaiacol to catechol, which is then catabolized by the beta-ketoadipate pathway.
Accumulation of 6-deoxyerythronolide B in a normal strain of Streptomyces erythreus and hydroxylation at carbon 6 of the erythranolide ring system by a soluble noninduced cell-free enzyme system.
Erythronolide B, a presumed intermediate in the biosynthesis of the erythromycins, has been shown to be formed from 6-deoxyerythronlide B by hydroxylation at C-6 and correlates well with the specific content of a cytochrome P-450 moiety present in the system and is inhibited by anaerobiosis and carbon monoxide.
The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.
High-performance liquid chromatography technique for resolving multiple forms of hepatic membrane-bound cytochrome P-450.
  • A. Kotake, Y. Funae
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1980
The results suggested that it is possible to separate membrane-bound proteins without dramatically altering their physical properties.