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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… (More)

Topic mentions per year

Topic mentions per year

1974-2017
010203019742017

Related topics

Related topics

11 relations

Broader (2)

Cytochrome P450Mixed Function Oxygenases
In BloodProcess of secretionadministration & dosageantagonists & inhibitors
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Related mentions per year

Related mentions per year

1936-2018
19401960198020002020
Camphor 5-Monooxygenase
physiological aspects
Cytochrome P450
Mixed Function Oxygenases
chemical synthesis
standards characteristics

Papers overview

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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… (More)
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2000
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… (More)
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Highly Cited
1997
Highly Cited
1997
The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
The substrate-bound structures of two cytochrome P450sf P450cam and P450eryF, are known. While these structures reveal important… (More)
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1997
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… (More)
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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… (More)
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1995
1995
Structure of cytochrome P450eryF involved in erythromycin biosynthesis
Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to… (More)
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1995
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… (More)
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1993
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… (More)
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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.
The substrate recognition regions in cytochrome P450 family 2 (CYP2) proteins were inferred by group-to-group alignment of CYP2… (More)
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Highly Cited
1987
Highly Cited
1987
High-resolution crystal structure of cytochrome P450cam.
The crystal structure of Pseudomonas putida cytochrome P450cam with its substrate, camphor, bound has been refined to R = 0.19 at… (More)
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