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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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2013
2013
The cytochrome P450 peroxygenases P450(Bsβ) (CYP152A1) from Bacillus subtilis and P450(Cla) (CYP152A2) from Clostridium… Expand
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Review
2012
Review
2012
Recent progress on the application of cytochrome P450 (P450) to bioconversion processes, biosensors, and bioremediation were… Expand
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2011
2011
Cytochrome P450(SPα) (CYP152B1) isolated from Sphingomonas paucimobilis is the first P450 to be classified as a H(2)O(2… Expand
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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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2010
2010
The modulation of peroxidase activity by fatty acid additives and organic cosolvents was determined and compared for four… Expand
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2009
2009
Cytochrome P450 enzymes are known to catalyze a variety of reactions that are difficult to perform by standard organic synthesis… Expand
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2002
2002
Cytochromes P450SP(alpha) (CYP152B1) and P450BS(beta) (CYP152A1), which are isolated from Sphingomonas paucimobilis and Bacillus… Expand
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2002
2002
Cytochrome P450 isolated from Bacillus subtilis (P450BSbeta; MW 48 kDa) catalyzes the hydroxylation of long-chain fatty acids at… Expand
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2001
2001
CYP152A1 is an unusual, peroxygenase enzyme that catalyzes the beta- or alpha-hydroxylation of fatty acids by efficiently… Expand
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