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Literature DB >> 19492389

A highly active single-mutation variant of P450BM3 (CYP102A1).

Christopher J C Whitehouse¹, Stephen G Bell, Wen Yang, Jake A Yorke, Christopher F Blanford, Anthony J F Strong, Edward J Morse, Mark Bartlam, Zihe Rao, Luet-Lok Wong.

Abstract

The power of proline: Bold amino acid substitutions in sensitive protein regions are frequently unproductive, while more subtle mutations can be sufficient to bring about dramatic changes. But introducing proline at the residue next to the sulfur ligand in P450(BM3) (CYP102A1) has the unexpected and desirable effect of enhancing the activity of this fatty acid hydroxylase with a broad range of non-natural substrates, as illustrated by the figure.

Entities: Chemical

Mesh：

Substances：

Year: 2009 PMID： 19492389 DOI： 10.1002/cbic.200900279

Source DB: PubMed Journal: Chembiochem ISSN： 1439-4227 Impact factor: 3.164

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Cited

17 in total

Review 1. Conformational plasticity and structure/function relationships in cytochromes P450.

Authors: Thomas C Pochapsky; Sophia Kazanis; Marina Dang
Journal: Antioxid Redox Signal Date: 2010-10 Impact factor: 8.401

2. Insights into electron leakage in the reaction cycle of cytochrome P450 BM3 revealed by kinetic modeling and mutagenesis.

Authors: Joseph B Lim; Kimberly A Barker; Kristen A Eller; Linda Jiang; Veronica Molina; Jessica F Saifee; Hadley D Sikes
Journal: Protein Sci Date: 2015-09-09 Impact factor: 6.725

3. Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies.

Authors: Jessica Spradlin; Diana Lee; Sruthi Mahadevan; Mavish Mahomed; Lawrence Tang; Quan Lam; Alexander Colbert; Oliver S Shafaat; David Goodin; Marco Kloos; Mallory Kato; Lionel E Cheruzel
Journal: Biochim Biophys Acta Date: 2016-09-14

Review 4. Use of chemical auxiliaries to control p450 enzymes for predictable oxidations at unactivated C-h bonds of substrates.

Authors: Karine Auclair; Vanja Polic
Journal: Adv Exp Med Biol Date: 2015 Impact factor: 2.622

5. Minor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates.

Authors: Francis K Yoshimoto; Yishan Zhou; Hwei-Ming Peng; David Stidd; Jennifer A Yoshimoto; Kamalesh K Sharma; Susan Matthew; Richard J Auchus
Journal: Biochemistry Date: 2012-08-27 Impact factor: 3.162

6. Stabilization of the Reductase Domain in the Catalytically Self-Sufficient Cytochrome P450_BM3 by Consensus-Guided Mutagenesis.

Authors: Gloria Saab-Rincón; Hanan Alwaseem; Valeria Guzmán-Luna; Leticia Olvera; Rudi Fasan
Journal: Chembiochem Date: 2018-02-12 Impact factor: 3.164

A highly active single-mutation variant of P450BM3 (CYP102A1).

Review 1. Conformational plasticity and structure/function relationships in cytochromes P450.

2. Insights into electron leakage in the reaction cycle of cytochrome P450 BM3 revealed by kinetic modeling and mutagenesis.

3. Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies.

Review 4. Use of chemical auxiliaries to control p450 enzymes for predictable oxidations at unactivated C-h bonds of substrates.

5. Minor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates.

6. Stabilization of the Reductase Domain in the Catalytically Self-Sufficient Cytochrome P450_BM3 by Consensus-Guided Mutagenesis.

Review 7. Cytochrome P450: taming a wild type enzyme.

8. Structural evidence: a single charged residue affects substrate binding in cytochrome P450 BM-3.

9. CYP261 enzymes from deep sea bacteria: a clue to conformational heterogeneity in cytochromes P450.

Review 10. Engineering cytochrome P450 biocatalysts for biotechnology, medicine and bioremediation.

A highly active single-mutation variant of P450BM3 (CYP102A1).

Review 1. Conformational plasticity and structure/function relationships in cytochromes P450.

2. Insights into electron leakage in the reaction cycle of cytochrome P450 BM3 revealed by kinetic modeling and mutagenesis.

3. Insights into an efficient light-driven hybrid P450 BM3 enzyme from crystallographic, spectroscopic and biochemical studies.

Review 4. Use of chemical auxiliaries to control p450 enzymes for predictable oxidations at unactivated C-h bonds of substrates.

5. Minor activities and transition state properties of the human steroid hydroxylases cytochromes P450c17 and P450c21, from reactions observed with deuterium-labeled substrates.

6. Stabilization of the Reductase Domain in the Catalytically Self-Sufficient Cytochrome P450BM3 by Consensus-Guided Mutagenesis.

Review 7. Cytochrome P450: taming a wild type enzyme.

8. Structural evidence: a single charged residue affects substrate binding in cytochrome P450 BM-3.

9. CYP261 enzymes from deep sea bacteria: a clue to conformational heterogeneity in cytochromes P450.

Review 10. Engineering cytochrome P450 biocatalysts for biotechnology, medicine and bioremediation.

6. Stabilization of the Reductase Domain in the Catalytically Self-Sufficient Cytochrome P450_BM3 by Consensus-Guided Mutagenesis.