Multiplicity of 3-Ketosteroid-9α-Hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.
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Pathogen roid rage: cholesterol utilization by Mycobacterium tuberculosisActivity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosisSubstrate Specificities and Conformational Flexibility of 3-Ketosteroid 9α-HydroxylasesMycobacterium smegmatis is a suitable cell factory for the production of steroidic synthonsCatabolism and biotechnological applications of cholesterol degrading bacteria.Unraveling and engineering the production of 23,24-bisnorcholenic steroids in sterol metabolism3-Ketosteroid 9α-hydroxylase enzymes: Rieske non-heme monooxygenases essential for bacterial steroid degradation.Genome-wide bioinformatics analysis of steroid metabolism-associated genes in Nocardioides simplex VKM Ac-2033D.Effect of methyl-β-cyclodextrin on gene expression in microbial conversion of phytosterol.Steroid Bioconversions.Structural features in the KshA terminal oxygenase protein that determine substrate preference of 3-ketosteroid 9α-hydroxylase enzymes.The essential function of genes for a hydratase and an aldehyde dehydrogenase for growth of Pseudomonas sp. strain Chol1 with the steroid compound cholate indicates an aldolytic reaction step for deacetylation of the side chainActinobacterial acyl coenzyme A synthetases involved in steroid side-chain catabolism.Functional differentiation of 3-ketosteroid Δ1-dehydrogenase isozymes in Rhodococcus ruber strain Chol-4.Gene cluster encoding cholate catabolism in Rhodococcus spp.Degradation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1 proceeds via an aldehyde intermediate.Biosynthesis of 1α-hydroxycorticosterone in the winter skate Leucoraja ocellata: evidence to suggest a novel steroidogenic route.Evidence of distinct pathways for bacterial degradation of the steroid compound cholate suggests the potential for metabolic interactions by interspecies cross-feeding.Molecular characterization of a new gene cluster for steroid degradation in Mycobacterium smegmatis.The effect of 3-ketosteroid-Δ(1)-dehydrogenase isoenzymes on the transformation of AD to 9α-OH-AD by Rhodococcus rhodochrous DSM43269.Influence of temperature on nucleus degradation of 4-androstene-3, 17-dione in phytosterol biotransformation by Mycobacterium sp.New Insights on Steroid Biotechnology.Comparative genomic analysis of Mycobacterium neoaurum MN2 and MN4 substrate and product tolerance.Functional analyses of three acyl-CoA synthetases involved in bile acid degradation in Pseudomonas putida DOC21
P2860
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P2860
Multiplicity of 3-Ketosteroid-9α-Hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.
description
2011 nî lūn-bûn
@nan
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@en
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@nl
type
label
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@en
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@nl
prefLabel
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@en
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@nl
P2093
P2860
P356
P1476
Multiplicity of 3-Ketosteroid- ...... different classes of steroids.
@en
P2093
Gerda Hessels
Mirjan Petrusma
Robert van der Geize
P2860
P304
P356
10.1128/JB.00274-11
P577
2011-06-03T00:00:00Z