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Camphor 5-Monooxygenase

Known as: Cytochrome P-450(cam), Camphor 5-Monooxygenase [Chemical/Ingredient], Cytochrome P450(cam) 
A soluble cytochrome P-450 enzyme that catalyzes camphor monooxygenation in the presence of putidaredoxin, putidaredoxin reductase, and molecular… Expand
National Institutes of Health

Related topics

Related topics

9 relations

Broader (2)

Cytochrome P450Mixed Function Oxygenases
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects
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Papers overview

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Highly Cited
2005
Highly Cited
2005
PELE:  Protein Energy Landscape Exploration. A Novel Monte Carlo Based Technique.
Combining protein structure prediction algorithms and Metropolis Monte Carlo techniques, we provide a novel method to explore all… Expand
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Highly Cited
2000
Highly Cited
2000
The catalytic pathway of cytochrome p450cam at atomic resolution.
Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at… Expand
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Highly Cited
2000
Highly Cited
2000
How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms.
Cytochrome P450s form a ubiquitous protein family with functions including the synthesis and degradation of many physiologically… Expand
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Review
1999
Review
1999
How similar are P450s and what can their differences teach us?
Cytochromes P450 form a very large superfamily of proteins which metabolize substrates from steroids to fatty acids to drugs and… Expand
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Highly Cited
1997
Highly Cited
1997
Alanine-scanning mutagenesis of a putative substrate recognition site in human cytochrome P450 3A4. Role of residues 210 and 211 in flavonoid activation and substrate specificity.
Alanine-scanning mutagenesis was performed on amino acid residues 210-216 of cytochrome P450 3A4, the major drug-metabolizing… Expand
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Highly Cited
1995
Highly Cited
1995
Structure and function of cytochromes P450: a comparative analysis of three crystal structures.
BACKGROUND Cytochromes P450 catalyze the oxidation of a variety of hydrophobic substrates. Sequence identities between P450… Expand
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Highly Cited
1995
Highly Cited
1995
A three-dimensional model of aromatase cytochrome P450.
P450 hemeproteins comprise a large gene superfamily that catalyzes monooxygenase reactions in the presence of a redox partner… Expand
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Highly Cited
1993
Highly Cited
1993
Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.
Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein… Expand
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Highly Cited
1992
Highly Cited
1992
Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences.
  • Osamu Gotoh
  • The Journal of biological chemistry
  • 1992
    • Corpus ID: 1408746
The substrate recognition regions in cytochrome P450 family 2 (CYP2) proteins were inferred by group-to-group alignment of CYP2… Expand
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Highly Cited
1986
Highly Cited
1986
Cytochrome P-450
ing species placed symmetrically between the endo and exo hydrogens could result in a G value of I, with subsequent asymmetric… Expand
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  • table VIII
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