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Camphor 5-Monooxygenase
Known as:
Cytochrome P-450(cam)
, Camphor 5-Monooxygenase [Chemical/Ingredient]
, Cytochrome P450(cam)
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A soluble cytochrome P-450 enzyme that catalyzes camphor monooxygenation in the presence of putidaredoxin, putidaredoxin reductase, and molecular…
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National Institutes of Health
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Related topics
Related topics
9 relations
Broader (2)
Cytochrome P450
Mixed Function Oxygenases
In Blood
Process of secretion
antagonists & inhibitors
aspects of radiation effects
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2010
Review
2010
P450 enzymes: their structure, reactivity, and selectivity-modeled by QM/MM calculations.
S. Shaik
,
Shimrit Cohen
,
Yong Wang
,
Hui Chen
,
Devesh Kumar
,
W. Thiel
Chemical reviews
2010
Corpus ID: 206903117
ion from camphor is affected by the choices made during setup.131 In this context, it should be noted that early QM/MM work on…
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Highly Cited
2001
Highly Cited
2001
Hydroxylation of camphor by reduced oxy-cytochrome P450cam: mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes.
R. Davydov
,
T. Makris
,
V. Kofman
,
D. Werst
,
S. Sligar
,
B. Hoffman
Journal of the American Chemical Society
2001
Corpus ID: 24781844
We have employed gamma-irradiation at cryogenic temperatures (77 K and also approximately 6 K) of the ternary complexes of…
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Highly Cited
2000
Highly Cited
2000
The catalytic pathway of cytochrome p450cam at atomic resolution.
I. Schlichting
,
J. Berendzen
,
+7 authors
S. Sligar
Science
2000
Corpus ID: 41635144
Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at…
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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
Huiying Li
,
T. Poulos
Nature Structural Biology
1997
Corpus ID: 27294690
The substrate-bound structures of two cytochrome P450sf P450cam and P450eryF, are known. While these structures reveal important…
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Highly Cited
1995
Highly Cited
1995
Structure and function of cytochromes P450: a comparative analysis of three crystal structures.
C. Hasemann
,
R. Kurumbail
,
S. Boddupalli
,
J. Peterson
,
J. Deisenhofer
Structure
1995
Corpus ID: 22489445
Highly Cited
1995
Highly Cited
1995
Structure of cytochrome P450eryF involved in erythromycin biosynthesis
J. Cupp-Vickery
,
T. Poulos
Nature Structural Biology
1995
Corpus ID: 22536232
Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to…
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Highly Cited
1993
Highly Cited
1993
Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's.
K. Ravichandran
,
S. Boddupalli
,
C. A. Hasermann
,
J. Peterson
,
J. Deisenhofer
Science
1993
Corpus ID: 45456088
Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein…
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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.
O. Gotoh
The Journal of biological chemistry
1992
Corpus ID: 1408746
Highly Cited
1987
Highly Cited
1987
High-resolution crystal structure of cytochrome P450cam.
T. Poulos
,
B. Finzel
,
A. Howard
Journal of molecular biology
1987
Corpus ID: 22732515
Highly Cited
1986
Highly Cited
1986
Cytochrome P-450
P. R. Montellano
Springer US
1986
Corpus ID: 197683
ing species placed symmetrically between the endo and exo hydrogens could result in a G value of I, with subsequent asymmetric…
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