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Page 32 of Cellular and Molecular Life Sciences Vol. 57, Issue 3
[page]
2000
Cellular and Molecular Life Sciences
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Chem
of amino acid and coding nucleotide sequences. J 267: 83-90
Lewis D. I and Moereels H. (1992) The sequence homologies of cytochromes P-450 and active-site Aided. Mol. Des. 6: 235-252 Korzekwa K. ...
S., Peterson ind function of
structures
3
3
Molecular modeling of P450s
(1989) a model-building study
Ferenczy G. G. and Morris G. M The active-site of cytochrome P-450 nifedipine oxidase J. Mol. ...
Metabolic tuning
1991
Nature
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Baldwin et al.
192 were able to use the high-resolution crystal structure of cytochrome P-450 bound to its camphor substrate, but had to model the putidaredoxin by sequence homology with a ferredoxin ...
The intermediate aromatic amino-acid residues crucial to the scheme of covalent switching (Fig. 2) are conserved among the many cytochromes whose sequence is known; most eukaryotic cytochromes P-450 ...
doi:10.1038/354192a0
fatcat:uecgzbabenaajpjjc6iava5bpe
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450
1985
Journal of Biological Chemistry
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The crystal structure of Pseudomonas putida cytochrome P-450cam in the ferric, camphor bound form has been determined and partially refined to R = 0.23 at 2.6 A. ...
The camphor is oriented such that the exo-surface of C5 would contact an iron bound, "activated" oxygen atom for stereoselective hydroxylation. ...
As a consequence of the homology in active site properties and the availability of diffraction quality crystals (13), the high resolution x-ray structure of P-45Ocam should provide a sound molecular basis ...
pmid:4066706
fatcat:754hx4oc4nfh3b7oeazehloq3q
Contents to volume 181
1985
FEBS Letters
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Guerra 291 W-NMR study of the interaction of aminopyrine with purified rat liver microsomal cytochrome P-450 (FEBS 2288) Yu. Yu. Woldman, L.M. Weiner, L.F. Gulyaeva, V. V. ...
Howden I54 Partial sequence homology of human myc oncogene protein to beta and gamma crystaltins (FEBS 2253) M.J.C. ...
doi:10.1016/0014-5793(85)80304-5
fatcat:z624lefn3vgdplm4lzax3dvwa4
The stereochemistry of peroxidase catalysis
1980
Journal of Biological Chemistry
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The indole ring of Trp-01 on the distal side of the heme ring i s probably the site of radical formation in compound I of cytochrome c peroxidase. ...
It is based on the 2.5 A structure of cytochrome c peroxidase, model building experiments, and an extensive body of literature on peroxidase biochemistry. ...
Acknowledgments-We wish to acknowledge the Chemistry Department Computing Facility and especially the expertise of Stephen Dempsey for his continued development of the Picture System. ...
pmid:6251047
fatcat:q4ymj4dtn5d5fc4rvrqsna42y4
Homology modeling a fast tool for drug discovery: Current perspectives
2012
Indian Journal of Pharmaceutical Sciences
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The recent advances in homology modeling, particularly in detecting and aligning sequences with template structures, distant homologues, modeling of loops and side chains as well as detecting errors in ...
.: Homology Modeling and Drug Discovery Major goal of structural biology involve formation of protein-ligand complexes; in which the protein molecules act energetically in the course of binding. ...
[170] used human cytochrome P 450 2C8 (CYP2C8) as template and created human cytochrome P 450 2C11 (CYP2C11) and human cytochrome P 450 2C13 (CYP2C13) models. ...
doi:10.4103/0250-474x.102537
pmid:23204616
pmcid:PMC3507339
fatcat:axgvmmgntfbenmcs7demtzuwme
Spectroscopic Characterization of a Green Copper Site in a Single-Domain Cupredoxin
2014
PLoS ONE
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Based on several spectroscopic and structural analyses, a connection between the geometry of their copperbinding site and their color has been proposed. ...
However, little is known about the relationship between such diversity of copper center geometry in cupredoxins and possible implications for function. ...
The Proteomic Analysis Center of IFR88 is part of MaP (Marseille Protéomique, IBiSA). The authors are grateful to the EPR facilities available at the Aix-Marseille University EPR center. ...
doi:10.1371/journal.pone.0098941
pmid:24932914
pmcid:PMC4059628
fatcat:7xy5kn63zre3zc6hhle76zdxjq
Cell biology and molecular basis of denitrification
1997
Microbiology and Molecular Biology Reviews
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The activation and enzymatic transformation of N oxides is based on the redox chemistry of Fe, Cu, and Mo. ...
assembly, and the biosynthesis of the cofactors molybdopterin and heme D1. ...
Dissimilatory NO Reductase The enzyme responsible for the conversion of NO to N 2 O is a cytochrome P-450 labeled with the epithet "nor" to distinguish it from other members of the cytochrome P-450 family ...
pmid:9409151
pmcid:PMC232623
fatcat:dl2aoyhjf5agfjmhsev55dyrmq
A predicted structure of the cytochrome c oxidase from Burkholderia pseudomallei
2003
Electronic Journal of Biotechnology
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(BIOTEK), Ministry of Science, Technology and the Environment, Malaysia. ...
Acknowledgments Computational facilities and resources used were based at the Bioinformatics Laboratory of the National Biotechnology and Bioinformatics Network (NBBnet), National Biotechnology Directorate ...
The cytochrome c oxidase bind two additional copper ions in the Cu A site to conserved histidine and cysteine residues of subunit II. ...
doi:10.2225/vol6-issue1-fulltext-5
fatcat:bsusnomtavasvhmboajofj66vq
Engineering, expression, and purification of "soluble" human cytochrome P45017α and its functional characterization
2008
Biochemistry (Moscow)
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This microsomal hemeprotein is unique in its ability to catalyze two independent reactions at the same active site. ...
We have constructed and purified the following mutant forms of human CYP17: CYP17dH (CYP17 with deleted hydrophobic N-terminal sequence (∆ 23 )) and CYP17mod (CYP17dH with substituted cluster of hydrophobic ...
and homology of the amino acid sequences of the two hemeproteins is 30%. ...
doi:10.1134/s0006297908070092
pmid:18707589
fatcat:ahggcnfx3rfzjidl7luc2jxgkm
Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds
1997
Biochemical Journal
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John Miles for providing the expression systems for cytochrome P-450 BM3 and its haem domain, to Gavain Sweetman and John Lamb for assistance with mass spectrometry, and to GlaxoWellcome and the Medical ...
It contains a P-450 haem domain and an NADPH-cytochrome P-450 reductase flavoprotein domain in a single polypeptide chain (M r 118 000), both of which show clear sequence homology with the corresponding ...
(These comparisons have been made between, for example, myristate and C "% TMA ; as discussed below, in terms of the active-site geometry this may not be an exact comparison.) ...
doi:10.1042/bj3270537
pmid:9359427
pmcid:PMC1218827
fatcat:7nb535b5ovc3tdrf63ktkljjvu
A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states
1994
Journal of Biological Chemistry
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Sequence analysis of the N terminus and the two heme-containing peptides generated by digestion of the enzyme with trypsin show 40% homology overall to sequences reported for the di-heme peroxidase from ...
Both the fully oxidized and half-reduced oxidation states of cytochrome c553 peroxidase are catalytically active as evidenced by the enzyme's ability to oxidize horse heart cytochrome c in the presence ...
Partial amino acid sequences of N. europaea cytochrome cm peroxidase and alignment with homologous regions in €? aemginosa cytochrome c661 peroxidase. ...
pmid:8163487
fatcat:mvi6a6vwcfgxpf7v2e6jwwlexa
Constrained water access to the active site of cytochrome P450 from the piezophilic bacteriumPhotobacterium profundum
2010
High Pressure Research
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We also demonstrate that saturated and unsaturated fatty acids exert opposite effects on solvent accessibility and hydration of the active site. ...
Comparison of P450-SS9 with cytochrome P450BM-3, a mesophilic fatty acid hydroxylase, suggests that P450-SS9 is characterized by severely confined accessibility and low water occupancy of the active site ...
We highly appreciate a kind gift of the purified heme domain of cytochrome P450BM-3 provided by Dr. Donovan C. Haines (Sam Houston State University, Huntsville, TX). ...
doi:10.1080/08957959.2010.535208
pmid:21475616
pmcid:PMC3070315
fatcat:2k4gm5f4sjdvjceqhyfnybs3qm
Molecular Modeling and Docking Analysis of CYP1A1 Associated with Head and Neck Cancer to Explore its Binding Regions
2014
Journal of Theoretical and Computational Science
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Phase I enzymes are mainly of cytochrome super family P-450 (CYP) that convert many compounds into highly reactive metabolites. ...
Abstract Cytochrome P450, family 1, subfamily A, polypeptide 1 is a phase I enzyme of cytochrome super family P-450 (CYP) involved in detoxification or conversion of carcinogens into a more electrophilic ...
doi:10.4172/2376-130x.1000112
fatcat:n6ffxg3dnnc2raneasnikjjgzi
Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b
2008
Protein Science
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The two irons of the active site cluster of MMOH OB3b are bridged by two OH (or one OH and one H20), as well as both carboxylate oxygens of Glu a144. ...
The high-resolution structure of MMOH OB3b indicates 26 consecutive amino acid sequence differences in the p chain when compared to the previously reported sequence inferred from the cloned gene. ...
Figure 7B shows the active site of cytochrome P-45oCAM oriented to emphasize this similar geometry. ...
doi:10.1002/pro.5560060305
pmid:9070438
pmcid:PMC2143674
fatcat:5ikazwufc5c4xphypzh75lsvyu
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