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cytochrome P-450 CYP152A1 (Bacillus subtilis)

Known as: CYP152A1, P450BSbeta, fatty acid beta-hydroxylase, CYP152A1 
National Institutes of Health

Papers overview

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Review
2018
Review
2018
The cytochromes P450 (P450s or CYPs) constitute a large heme enzyme superfamily, members of which catalyze the oxidative… Expand
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2013
2013
The cytochrome P450 peroxygenases P450Bsβ (CYP152A1) from Bacillus subtilis and P450Cla (CYP152A2) from Clostridium… Expand
Review
2012
Review
2012
  • T. Sakaki
  • Biological & pharmaceutical bulletin
  • 2012
  • Corpus ID: 25740380
Recent progress on the application of cytochrome P450 (P450) to bioconversion processes, biosensors, and bioremediation were… Expand
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Highly Cited
2011
Highly Cited
2011
Cytochrome P450(SPα) (CYP152B1) isolated from Sphingomonas paucimobilis is the first P450 to be classified as a H(2)O(2… Expand
Review
2010
Review
2010
Cytochrome P450 enzymes (P450s) are able to regioselectively and stereoselectively introduce oxygen into organic compounds under… Expand
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2009
2009
The big screen: We have devised a high‐throughput screening method for organic peroxide‐dependent P450 reactivity by taking… Expand
Highly Cited
2002
Highly Cited
2002
Cytochromes P450SP(alpha) (CYP152B1) and P450BS(beta) (CYP152A1), which are isolated from Sphingomonas paucimobilis and Bacillus… Expand
2002
2002
Cytochrome P450 isolated from Bacillus subtilis (P450BSbeta; MW 48 kDa) catalyzes the hydroxylation of long-chain fatty acids at… Expand
Highly Cited
2001
Highly Cited
2001
CYP152A1 is an unusual, peroxygenase enzyme that catalyzes the beta- or alpha-hydroxylation of fatty acids by efficiently… Expand