1,019 Hits in 9.0 sec

Page 32 of Cellular and Molecular Life Sciences Vol. 57, Issue 3 [page]

2000 Cellular and Molecular Life Sciences  
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

David Jones
1991 Nature  
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

T L Poulos, B C Finzel, I C Gunsalus, G C Wagner, J Kraut
1985 Journal of Biological Chemistry  
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  
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

T L Poulos, J Kraut
1980 Journal of Biological Chemistry  
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

VK Vyas, RD Ukawala, C Chintha, M Ghate
2012 Indian Journal of Pharmaceutical Sciences  
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

Magali Roger, Frédéric Biaso, Cindy J. Castelle, Marielle Bauzan, Florence Chaspoul, Elisabeth Lojou, Giuliano Sciara, Stefano Caffarri, Marie-Thérèse Giudici-Orticoni, Marianne Ilbert, Vladimir N. Uversky
2014 PLoS ONE  
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

W G Zumft
1997 Microbiology and Molecular Biology Reviews  
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

Rahmah Mohamed, Mohd Firdaus-Raih, Ahmad Tarmidi Sailan, Zulkeflie Zamrod, Mohd. Noor Embi
2003 Electronic Journal of Biotechnology  
(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

T. A. Pechurskaya, O. P. Lukashevich, A. A. Gilep, S. A. Usanov
2008 Biochemistry (Moscow)  
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

F. Catherine OLIVER, Sandeep MODI, U. William PRIMROSE, Lu-Yun LIAN, C. K. Gordon ROBERTS
1997 Biochemical Journal  
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

D M Arciero, A B Hooper
1994 Journal of Biological Chemistry  
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

Elena V. Sineva, Dmitri R. Davydov
2010 High Pressure Research  
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

Sheikh Arslan Sehgal, Rana Adnan Tahir
2014 Journal of Theoretical and Computational Science  
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

Nates An Elango, Ramaswamy Radhakrishnan, Wayne A. Froland, Bradley J. Wallar, Cathleen A. Earhart, John D. Lipscomb, Douglas H. Ohlendorf
2008 Protein Science  
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
« Previous Showing results 1 — 15 out of 1,019 results