Structure and function of cytochromes P450:a comparative analysis of three crystal structures

Structure

Volumn 3, Issue 1, 1995, Pages 41-62

  Hasemann, Charles A ^a   Kurumbail, Ravi G ^a   Boddupalli, Sekhar S ^a   Peterson, Julian A ^b   Deisenhofer, Johann ^b  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

crystal structure; cytochrome P450; electrostatics; hemoprotein; monooxygenase

Indexed keywords

CYTOCHROME P 450 ENZYME SYSTEM; CYTOCHROME P450;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; COMPUTER GRAPHICS; HUMAN; METABOLISM; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; COMPARATIVE STUDY; COMPUTER GRAPHICS; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; HUMAN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

EID: 0029643786     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00134-4     Document Type: Article

References (91)

1. Reactions and significance of cytochrome P-450 enzymes
2. Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms
3. The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes and nomenclature
4. Cytochromes P-450 and the regulation of steroid synthesis
5. The human hepatic cytochromes P450 involved in drug metabolism
6. P450 and human cancer
7. Cytochrome P450 and the arachidonate cascade
8. Prostaglandin metabolism by hepatic cytochrome P-450
9. Mechanisms of cytochrome P450 and peroxidase-catalyzed xenobiotic metabolism
10. The 26 Å crystal structure of Pseudomonas putida cytochrome P-450
11. Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
12. cam
13. cam ternary complex
14. cam
15. Inhibitor-induced conformational change in cytochrome P-450cam
16. CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation
17. cam iron–phenyl complex
18. cam
19. Crystal structure of the cytochrome P-450cam active site mutant Thr252Ala
20. cam : crystallography, oxygen activation, and electron transfer
21. terp at 2.3 Å resolution
22. BM-3 , a prototype for microsomal P450s
23. terp . Isolation and purification of the protein and cloning and sequencing of its operon
24. BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation
25. BM-3 utilizing individual recombinant hemo–and flavoprotein domains
26. The protein data bank: a computer-based archival file for macromolecular structures
27. The relation between the divergence of sequence and structure in proteins
28. Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
29. On the membrane topology of vertebrate cytochrome P-450 proteins
30. cam
31. A predicted three-dimensional structure of human cytochrome P450: implications for substrate specificity
32. Secondary structure and membrane topology of cytochrome P450s
33. cam — indications for a similar overall topology
34. The sequence homologies of cytochromes P-450 and active site geometries
35. cam
36. A theoretical model for the effects of local nonpolar heme environments on the redox potentials in cytochromes
37. Structure and function of the constant regions of immunoglobulins
38. Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center
39. The structure function and evolution of cytochromes
40. cam : a network connecting the heme group with helix K
41. 17α
42. Functional domains of aromatase cytochrome P450 inferred from comparative analyses of amino acid sequences and substantiated by site-directed mutagenesis experiments
43. d by site-directed mutagenesis. Interaction with NADPH-cytochrome P450 reductase
44. d : catalytic activities toward benzphetamine and 7-ethoxycoumarin
45. BM-3
46. cam as revealed by site-directed mutagenesis
47. 106 and P450 reductase
48. max of the enzyme for bufuralol but not debrisoquine hydroxylation
49. coh substrate specificity by mutation of a single amino-acid residue
50. Hybrid cytochromes P-450 identify a substrate binding domain in P-450IIC5 and P-450IIC4
51. Sequence requirements for cytochrome P-450IIB1 catalytic activity. Alteration of the stereospecificity and regioselectivity of steroid hydroxylation by a simultaneous change of two hydrophobic amino acid residues to phenylalanine
52. Engineering of cytochrome P450 2B1 specificity. Conversion of an androgen 16β–hydroxylase to a 15α–hydroxylase
53. cam to increase the stereospecificity and coupling of aliphatic hydroxylation
54. Engineering mouse P450coh to a novel corticosterone 15α–hydroxylase and modeling steroid-binding orientation in the substrate pocket
55. Structural function of residue-209 in coumarin 7-hydroxylase (P450coh). Enzyme-kinetic studies and site-directed mutagenesis
56. A comprehensive set of sequence analysis programs for the VAX
57. Replacement of Thr-303 of P450 2E1 with serine modifies the regioselectivity of its fatty acid hydroxylase activity
58. Site-directed mutagenesis of cytochromes CYP2A1 and CYP2A2: influence of the distal helix on the kinetics of testosterone hydroxylation
59. Structure–function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis
60. A site-directed mutagenesis study of human placental aromatase
61. A single amino acid substitution confers progesterone 6β–hydroxylase activity to rabbit cytochrome P450 2C3
62. Role of residue 478 as a determinant of the substrate specificity of cytochrome P450 2B1
63. Oxygen activation by cytochrome P-450
64. Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate
65. Catalytic mechanism of cytochrome P-450: evidence for a distal charge relay
66. cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: a possible role of the hydroxy amino acid in oxygen activation
67. d
68. Point mutations at threonine-301 modify substrate specificity of rabbit liver microsomal cytochromes P-450 (laurate (ω–1)-hydroxylase and testosterone 16α–hydroxylase)
69. Equilibrium and kinetic studies of the interaction of cytochrome P-450cam and putidaredoxin
70. Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle
71. 5 and cytochrome P-450 reductase with cytochrome P-450 in the membrane of reconstituted vesicles
72. cam binding surface as defined by site-directed mutagenesis and electrostatic modeling
73. cam electron-transfer complex
74. cam for electron transfer from reduced putidaredoxin
75. Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding
76. Modification of carboxyl groups on NADPH-cytochrome P-450 reductase involved in binding of cytochromes c and P-450 LM2
77. scc
78. Identification of specific carboxylate groups on adrenodoxin that are involved in the interaction with adrenodoxin reductase
79. The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase
80. An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
81. Faster superoxide dismutase mutants designed by enhancing electrostatic guidance
82. The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane
83. Membrane topology of the mammalian P450 cytochromes
84. O: a macromolecule modeling environment
85. Profile analysis: detection of distantly related proteins
86. Three-dimensional profiles from residue-pair preferences: identification of sequences with β/α–barrel fold
87. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino-acid modification