Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form-Reference-Cited by-同舟云学术

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Crystal Structure of CYP106A2 in Substrate-Free and Substrate-Bound Form

Published:2016-03-11 Issue:9 Volume:17 Page:852-860
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Janocha Simon¹,Carius Yvonne²,Hutter Michael³,Lancaster C. Roy D.²,Bernhardt Rita¹

Affiliation:

1. Department of Biochemistry; Saarland University; Campus B2.2 66123 Saarbrücken Germany

2. Department of Structural Biology, ZHMB; Saarland University; Building 60 66421 Homburg Germany

3. Center for Bioinformatics; Saarland University; Campus E2.1 66123 Saarbrücken Germany

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference55 articles.

1. Cytochrome P450: Structure, function, and generation of reactive oxygen species

2. Cytochromes P450 as versatile biocatalysts

3. Cytochromes P450 as promising catalysts for biotechnological application: chances and limitations

4. Crystal Structure of Albaflavenone Monooxygenase Containing a Moonlighting Terpene Synthase Active Site

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1. Evidential deep learning for trustworthy prediction of enzyme commission number;Briefings in Bioinformatics;2023-11-22

2. Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2;Journal of Inorganic Biochemistry;2023-04

3. Crystal Structure and Biochemical Analysis of a Cytochrome P450 Steroid Hydroxylase (BaCYP106A6) from Bacillus Species;Journal of Microbiology and Biotechnology;2022-12-12

4. Structural comparison of the cytochrome P450 enzymes CYP106A1 and CYP106A2 provides insight into their differences in steroid conversion;FEBS Letters;2022-10-06

5. Cytochrome P450 Monooxygenases Catalyse Steroid Nucleus Hydroxylation with Regio‐ and Stereo‐Selectivity;Advanced Synthesis & Catalysis;2022-07-20

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