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Literature DB >> 22890798

Rates of fatty acid oxidations by P450 compound I are pH dependent.

Abstract

The rates of oxidation of fatty acids by CYP119 compound I were dependent on the pH of the medium. The plot shows log k values for reactions of acids as a function of pH, where the slopes indicate mixed third-order and fourth-order dependence on base concentration. For palmitic acid, the rate increased 50-fold over the pH range 6.8-7.3.

Entities: Chemical Disease Gene Species

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Year: 2012 PMID： 22890798 PMCID： PMC3477493 DOI： 10.1002/cbic.201200387

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

14 in total

1. Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus.

Authors: J K Yano; L S Koo; D J Schuller; H Li; P R Ortiz de Montellano; T L Poulos
Journal: J Biol Chem Date: 2000-10-06 Impact factor: 5.157

2. Heme-Containing Oxygenases.

Authors: Masanori Sono; Mark P. Roach; Eric D. Coulter; John H. Dawson
Journal: Chem Rev Date: 1996-11-07 Impact factor: 60.622

3. Rate-controlling isomerizations in fatty acid oxidations by a cytochrome P450 compound I.

Authors: Zhi Su; Xiaohong Chen; John H Horner; Martin Newcomb
Journal: Chemistry Date: 2012-02-01 Impact factor: 5.236

4. Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics.

Authors: Jonathan Rittle; Michael T Green
Journal: Science Date: 2010-11-12 Impact factor: 47.728

5. Role of hemoprotein P-450 in fatty acid omega-hydroxylation in a soluble enzyme system from liver microsomes.

Authors: A Y Lu; M J Coon
Journal: J Biol Chem Date: 1968-03-25 Impact factor: 5.157

6. Kinetic characterization of compound I formation in the thermostable cytochrome P450 CYP119.

Authors: David G Kellner; Shao-Ching Hung; Kara E Weiss; Stephen G Sligar
Journal: J Biol Chem Date: 2002-01-17 Impact factor: 5.157

Review 7. Spectroscopic characterization of cytochrome P450 Compound I.

Authors: Christiane Jung; Simon de Vries; Volker Schünemann
Journal: Arch Biochem Biophys Date: 2010-12-30 Impact factor: 4.013

8. Spectroscopic investigations of intermediates in the reaction of cytochrome P450(BM3)-F87G with surrogate oxygen atom donors.

Authors: Gregory M Raner; Jonathan I Thompson; Alice Haddy; Valary Tangham; Nicole Bynum; G Ramachandra Reddy; David P Ballou; John H Dawson
Journal: J Inorg Biochem Date: 2006-10-07 Impact factor: 4.155

Rates of fatty acid oxidations by P450 compound I are pH dependent.

1. Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus.

2. Heme-Containing Oxygenases.

3. Rate-controlling isomerizations in fatty acid oxidations by a cytochrome P450 compound I.

4. Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics.

5. Role of hemoprotein P-450 in fatty acid omega-hydroxylation in a soluble enzyme system from liver microsomes.

6. Kinetic characterization of compound I formation in the thermostable cytochrome P450 CYP119.

Review 7. Spectroscopic characterization of cytochrome P450 Compound I.

8. Spectroscopic investigations of intermediates in the reaction of cytochrome P450(BM3)-F87G with surrogate oxygen atom donors.

Review 9. Hydrocarbon hydroxylation by cytochrome P450 enzymes.

10. A highly reactive p450 model compound I.

1. Driving force for oxygen-atom transfer by heme-thiolate enzymes.

2. Synthesis of ω-hydroxy dodecanoic acid based on an engineered CYP153A fusion construct.