메뉴 건너뛰기
Current Opinion in Structural Biology
Volumn 5, Issue 6, 1995, Pages 767-774
Cytochrome P450
Author keywords

[No Author keywords available]
Indexed keywords

CYTOCHROME P450; HEME DERIVATIVE;
EID: 0029584687     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0959-440X(95)80009-3     Document Type: Article
Times cited : (94)
References (48)
  • 3
    • 0029137990 scopus 로고
    • BM-3
    • BM-3 heme domain. Energy-minimization studies on the refined crystal structure show that the substrate-access channel undergoes a very large conformational change going from an open conformation to a closed conformation more compatible with substrate binding. The local environment and intermolecular contacts hold the access channel open in the crystal lattice. This explains why soaking crystals in fatty acid substrates leads to either no detectable binding or crystal cracking.
    • (1995) Acta Crystallogr [D] , vol.51 , pp. 21-32
    • Li1    Poulos2
  • 5
    • 0029586252 scopus 로고
    • eryF involved in erythromycin biosynthesis
    • eryF structure also suggests the possible involvement of substrate-assisted acid catalysis in the molecular-oxygen activation step of the P450 catalytic cycle.
    • (1995) Nature Struct Biol , vol.2 , pp. 144-153
    • Cupp-Vickery1    Poulos2
  • 6
    • 0002783389 scopus 로고
    • BM-3, a catalytically self-sufficient monooxygenease induced by barbituates in Bacillus megaterium
    • (1987) J Biol Chem , vol.292 , pp. 6883-6890
    • Narhi1    Fulco2
  • 8
    • 0026500150 scopus 로고
    • Characterization of Saccharapolyspora erythraea cytochrome P450 genes and enzymes, including 6-deoxyerythronolide B hydroxylase
    • (1992) J Bacteriol , vol.174 , pp. 725-735
    • Andersen1    Hutchinson2
  • 11
    • 0028912205 scopus 로고
    • Expression of cytochrome P450 3A5 in E. coli: Effects of 5′ modification, purification, spectral characterization, reconstitution conditions, and catalytic activities
    • of special interest, These two papers [10,11], together with [9], focus on the expression of eukaryotic P450s in recombinant hosts. Of particular importance is the role of the hydrophobic N-terminal leader in partitioning between the membrane and cytosol as well as methods for solubilizing recombinantly expressed P450s.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 374-384
    • Gillam1    Guo2    Ueng3    Yamazaki4    Cock5    Reilly6    Hooper7    Guengerich8
  • 14
    • 0028084782 scopus 로고
    • Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 Å resolution
    • (1994) FEBS Letters , vol.339 , pp. 291-296
    • Peterson1    Kadiziola2    Larsen3
  • 16
  • 17
    • 0028773124 scopus 로고
    • Laue diffraction study of the structure of cytochrome c peroxidase compound I
    • of special interest, Laue diffraction is an old yet only recently employed technique for vastly increasing the amount of X-ray data that can be obtained from protein crystals by using a broad spectrum of X-ray wavelengths rather than the usual single wavelength. The growing interest in this method reflects an increasing availability of high intensity synchrotron X-ray sources which offer the possibility of obtaining nearly complete sets of X-ray intensity data at moderate-to-high resolution in very short periods of time (i.e. seconds). In this way the structures of important semi-transient enzyme intermediates may be obtained. This paper utilizes the method to obtain the structure of the relatively short-lived compound I intermediate formed upon reaction of the peroxidase with hydrogen peroxide. The Laue structure is basically the same as that obtained by more conventional methods which required six crystals [48].
    • (1994) Structure , vol.2 , pp. 201-208
    • Fulop1    Phizackerly2    Soltis3    Clifton4    Wakatsuki5    Erman6    Hajdu7    Edwards8
  • 19
    • 0028773636 scopus 로고
    • Comparative structural analysis of peroxidase and P450 crystal strutures
    • BM-3 (17% sequence identity). It is shown that the peroxidases exhibit a far more conservative structure than do the P450s. The differences are related to functional differences between the two classes of enzymes.
    • (1994) Structure , vol.2 , pp. 461-464
    • Li1    Poulos2
  • 21
    • 0028956684 scopus 로고
    • BM-3 by molecular dynamics simulations
    • BM-3 heme domain. The crystal form used for the structure determination has two molecules in the asymmetric unit. One molecule exhibits very large fluctuations in the substrate access channel whereas the other does not.
    • (1995) Proteins , vol.21 , pp. 237-243
    • Paulsen1    Ornstein2
  • 22
    • 0028109245 scopus 로고
    • Alterations of the regioselectivity of progesterone metabolism by the mutagenesis of two key amino acid residues in rabbit cytochrome P450 2C3v
    • (1994) J Biol Chem , vol.269 , pp. 23937-23943
    • Richardson1    Johnson2
  • 24
    • 0028103817 scopus 로고
    • Structure—function analysis of CYP2A10 and CYP2A11 cytochromes that differ in only eight amino acids but have strikingly different activities toward testosterone and courmarin
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 373-378
    • Ding1    Peng2    Coon3
  • 25
    • 0027457924 scopus 로고
    • Engineering of cytochrome P4502B1 Specificity
    • (1993) J Biol Chem , vol.268 , pp. 4453-4457
    • Halpert1    He2
  • 26
    • 0028968913 scopus 로고
    • Altering the regioselectivity of androstenedione hydroxylase activity in P450s 2a-4/5 by a mutation of the residue at position 481
    • of special interest, This paper provides a summary of mutations outside the B′ helix region that alter substrate regiospecificity. In particular the authors discuss mutations that map in the segment between the F/G loop and the ‘loop’ between two β-strands (see Fig. 1).
    • (1995) Biochemistry , vol.34 , pp. 5054-5059
    • Iwasaki1    Darden2    Pedersen3    Negishi4
  • 28
    • 0029170124 scopus 로고
    • cam
    • cam. The stability of the intermediate substrate radical is also shown to be an important factor in controlling regiospecificity [28]. The agreement between predicited substrate hydroxylation profiles and experimental data is quite good.
    • (1995) Journal of the American Chemical Society , vol.117 , pp. 2736-2746
    • Harris1    Loew2
  • 32
    • 0028527837 scopus 로고
    • An evaluation of molecular models of the cytochrome P450 Streptomyces griseolus enzymes P450SU1 and P450SU2
    • of special interest, In addition to predicting a P450 structure, this paper provides a useful analysis of modeling methods. The authors test the variation in the homology-modeled P450 structure as a function of sequence-alignment method and energy-minimization protocols. The authors find that the most unreliably modeled region lies within the B′ helix which is also important for controlling the size, shape and specificity of the substrate-binding pocket.
    • (1994) J Comput Aided Mol Des , vol.8 , pp. 607-622
    • Braatz1    Bass2    Ornstein3
  • 34
    • 0029033662 scopus 로고
    • A three-dimensional model of aromatase cytochrome P450
    • BM-3 as templates. This paper also offers a relatively bold and detailed description of how the androstenedione binds to the hypothetical model, in addition to a proposal for the catalytic mechanism.
    • (1995) Protein Sci , vol.4 , pp. 1065-1080
    • Graham-Lorence1    Amarneh2    White3    Peterson4    Simpson5
  • 35
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: a comparative analysis of three crystal structures
    • BM-3. Several important structurally conserved regions are noted and discussed in detail. Sequence alignments based on the crystal structures are especially interesting.
    • (1995) Structure , vol.3 , pp. 41-62
    • Hasemann1    Kurumbail2    Boddupalli3    Petereson4    Deisenhofer5
  • 36
    • 0028986232 scopus 로고
    • cam: a study with unnatural amino acid mutagenesis
    • 2 molecule. I have examined the possible consequences of this mutation by molecular modeling; it turns out that one extra methyl group can be readily accommodated with only a modest repositioning of groups in the immediate vicinity of the mutation.
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 96-102
    • Kimata1    Shimada2    Hirose3    Ishimura4
  • 40
    • 0028233575 scopus 로고
    • Differential roles for Glu318 and Thr319 in cytochrome P450 1A2 catalysis supported by NADPH-cytochrome P450 reductase and tert-butyl hydroperoxide
    • cam numbering scheme) in other eukaryotic P450s. The results are mixed but do show that this threonine is not a critical amino acid in all P450s.
    • (1994) Arch Biochem Biophys , vol.310 , pp. 397-401
    • Hiroya1    Murakami2    Shimizu3    Hatano4    Ortiz de Montellano5
  • 41
    • 0027994378 scopus 로고
    • cam oxygen activation
    • cam mutants. The activity of this mutant is significantly lower than that of the wild-type. In addition, an intriguing build-up of a new spectral intermediate is observed under steady-state conditions suggesting a change in the rate-limiting step. This system could provide an excellent opportunity to trap and study an important catalytic intermediate.
    • (1994) J Biol Chem , vol.269 , pp. 4260-4266
    • Gerber1    Sligar2
  • 46
    • 0027609916 scopus 로고
    • SETOR: hardware lighted three-dimensional solid model representations of macromolecules
    • (1993) J Mol Graphics , vol.11 , pp. 134-138
    • Evans1
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis1

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.