Engineering of Cytochrome P450 3A4 for Enhanced Peroxide-Mediated Substrate Oxidation Using Directed Evolution and Site-Directed Mutagenesis

Santosh Kumar; Hong Liu; James R. Halpert

doi:10.1124/dmd.106.012054

Engineering of Cytochrome P450 3A4 for Enhanced Peroxide-Mediated Substrate Oxidation Using Directed Evolution and Site-Directed Mutagenesis

Drug Metabolism and Disposition ◽

10.1124/dmd.106.012054 ◽

2006 ◽

Vol 34 (12) ◽

pp. 1958-1965 ◽

Cited By ~ 33

Author(s):

Santosh Kumar ◽

Hong Liu ◽

James R. Halpert

Keyword(s):

Cytochrome P450 ◽

Directed Evolution ◽

Substrate Oxidation ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Cytochrome P450 3A4

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Identification of Three Key Residues in Substrate Recognition Site 5 of Human Cytochrome P450 3A4 by Cassette and Site-Directed Mutagenesis†

Biochemistry ◽

10.1021/bi970182i ◽

1997 ◽

Vol 36 (29) ◽

pp. 8831-8839 ◽

Cited By ~ 60

Author(s):

You Ai He ◽

You Qun He ◽

Grazyna D. Szklarz ◽

James R. Halpert

Keyword(s):

Cytochrome P450 ◽

Substrate Recognition ◽

Recognition Site ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Cytochrome P450 3A4 ◽

Human Cytochrome ◽

Key Residues

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Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)67801-4 ◽

1991 ◽

Vol 266 (6) ◽

pp. 3372-3375

Author(s):

T Shimizu ◽

T Tateishi ◽

M Hatano ◽

Y Fujii-Kuriyama

Keyword(s):

Cytochrome P450 ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Cytochrome P450 Reductase ◽

Nadph Cytochrome ◽

P450 Reductase ◽

Catalytic Function ◽

Nadph Cytochrome P450 Reductase

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Functional domains of aromatase cytochrome P450 inferred from comparative analyses of amino acid sequences and substantiated by site-directed mutagenesis experiments.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)42294-0 ◽

1994 ◽

Vol 269 (2) ◽

pp. 1564

Author(s):

S. Chen ◽

D. Zhou

Keyword(s):

Cytochrome P450 ◽

Amino Acid ◽

Amino Acid Sequences ◽

Site Directed Mutagenesis ◽

Functional Domains ◽

Directed Mutagenesis ◽

Comparative Analyses

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Enhancing thermostabilization of a newly discovered α-amylase from Bacillus cereus GL96 by combining computer-aided directed evolution and site-directed mutagenesis

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2021.12.057 ◽

2021 ◽

Author(s):

Soroosh Pouyan ◽

Milad Lagzian ◽

Mohammad Hossein Sangtarash

Keyword(s):

Bacillus Cereus ◽

Directed Evolution ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Computer Aided

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Site-Directed Mutagenesis of Cytochrome P450eryF: Implications for Substrate Oxidation, Cooperativity, and Topology of the Active Site

Chemical Research in Toxicology ◽

10.1021/tx025539k ◽

2002 ◽

Vol 15 (6) ◽

pp. 843-853 ◽

Cited By ~ 15

Author(s):

Kishore K. Khan ◽

You Ai He ◽

You Qun He ◽

James R. Halpert

Keyword(s):

Active Site ◽

Substrate Oxidation ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

And Topology

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Improved Thermostability of Maltooligosyltrehalose Synthase fromArthrobacter ramosusby Directed Evolution and Site-Directed Mutagenesis

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.9b01123 ◽

2019 ◽

Vol 67 (19) ◽

pp. 5587-5595 ◽

Cited By ~ 5

Author(s):

Chun Chen ◽

Lingqia Su ◽

Fei Xu ◽

Yongmei Xia ◽

Jing Wu

Keyword(s):

Directed Evolution ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis

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Alteration of the substrate specificity of cytochrome P450 CYP199A2 by site-directed mutagenesis

Journal of Bioscience and Bioengineering ◽

10.1016/j.jbiosc.2014.05.028 ◽

2015 ◽

Vol 119 (1) ◽

pp. 47-51 ◽

Cited By ~ 8

Author(s):

Toshiki Furuya ◽

Yoh Shitashima ◽

Kuniki Kino

Keyword(s):

Cytochrome P450 ◽

Substrate Specificity ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis

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Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein-ligand interactions based on crystal structures of the ligand-bound enzyme

FEBS Journal ◽

10.1111/j.1742-4658.2011.08411.x ◽

2011 ◽

Vol 279 (9) ◽

pp. 1607-1620 ◽

Cited By ~ 24

Author(s):

P. Ross Wilderman ◽

Sean C. Gay ◽

Hyun-Hee Jang ◽

Qinghai Zhang ◽

C. David Stout ◽

...

Keyword(s):

Cytochrome P450 ◽

Crystal Structures ◽

Active Site ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Active Site Residues ◽

Protein Ligand Interactions ◽

Cytochrome P450 2B4 ◽

Ligand Interactions

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Evidence for the functional role of residues in the B′–C loop of baboon cytochrome P450 side-chain cleavage (CYP11A1) obtained by site-directed mutagenesis, kinetic analysis and homology modelling

The Journal of Steroid Biochemistry and Molecular Biology ◽

10.1016/j.jsbmb.2006.07.003 ◽

2007 ◽

Vol 103 (1) ◽

pp. 65-75 ◽

Cited By ~ 1

Author(s):

Karl-Heinz Storbeck ◽

Pieter Swart ◽

Sandra Graham ◽

Amanda C. Swart

Keyword(s):

Cytochrome P450 ◽

Kinetic Analysis ◽

Functional Role ◽

Homology Modelling ◽

Site Directed Mutagenesis ◽

Side Chain ◽

Directed Mutagenesis ◽

Side Chain Cleavage ◽

Chain Cleavage

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Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis.

Molecular Endocrinology ◽

10.1210/mend.7.12.8145767 ◽

1993 ◽

Vol 7 (12) ◽

pp. 1617-1624 ◽

Cited By ~ 1

Author(s):

B Amarneh ◽

C J Corbin ◽

J A Peterson ◽

E R Simpson ◽

S Graham-Lorence

Keyword(s):

Cytochrome P450 ◽

Site Directed Mutagenesis ◽

Functional Domains ◽

Directed Mutagenesis ◽

Human Aromatase ◽

Linear Alignment

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