Structural Evidence for Enhancement of Sequential Vitamin D3 Hydroxylation Activities by Directed Evolution of Cytochrome P450 Vitamin D3 Hydroxylase

Structural Evidence for Enhancement of Sequential Vitamin D3 Hydroxylation Activities by Directed Evolution of Cytochrome P450 Vitamin D3 Hydroxylase

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http://www.wikidata.org/entity/Q27663638
A single mutation at the ferredoxin binding site of P450 Vdh enables efficient biocatalytic production of 25-hydroxyvitamin D(3)Structure of the quinoline N-hydroxylating cytochrome P450 RauA, an essential enzyme that confers antibiotic activity on aurachin alkaloidsEnzyme-substrate complex structures of CYP154C5 shed light on its mode of highly selective steroid hydroxylationActive-site residues move independently from the rest of the protein in a 200 ns molecular dynamics simulation of cytochrome P450 CYP119.Diversity of P450 enzymes in the biosynthesis of natural productsDirected evolution of cytochrome P450 enzymes for biocatalysis: exploiting the catalytic versatility of enzymes with relaxed substrate specificity.Pursuing the unlimited potential of microorganisms-progress and prospect of a fermentation company.Biochemical and structural characterization of CYP109A2, a vitamin D3 25-hydroxylase from Bacillus megaterium.Cloning and heterologous expression of the aurachin RE biosynthesis gene cluster afford a new cytochrome P450 for quinoline N-hydroxylation.Identification of a vitamin D3-specific hydroxylase genes through actinomycetes genome mining.Engineering of a hybrid biotransformation system for cytochrome P450sca-2 in Escherichia coli.Semi-rational engineering of cytochrome P450sca-2 in a hybrid system for enhanced catalytic activity: insights into the important role of electron transfer.The catabolism of 3,6-Dichlorosalicylate is Initiated by the Cytochrome P450 Monooxygenase System DsmABC in Rhizorhabdus dicambivorans Ndbn-20.Structural insights into the mechanism of the drastic changes in enzymatic activity of the cytochrome P450 vitamin D3 hydroxylase (CYP107BR1) caused by a mutation distant from the active site.
P2860

Structural Evidence for Enhancement of Sequential Vitamin D3 Hydroxylation Activities by Directed Evolution of Cytochrome P450 Vitamin D3 Hydroxylase

Item
http://www.wikidata.org/entity/Q27663638
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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type
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
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P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932
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P1476
Structural Evidence for Enhanc ...... me P450 Vitamin D3 Hydroxylase
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932