Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2
about
Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2)Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlI, a cytochrome P450 of Streptomyces avermitilisCrystal structures and catalytic mechanism of cytochrome P450 StaP that produces the indolocarbazole skeletonMycobacterium tuberculosis CYP130: CRYSTAL STRUCTURE, BIOPHYSICAL CHARACTERIZATION, AND INTERACTIONS WITH ANTIFUNGAL AZOLE DRUGSDeterminants of Cytochrome P450 2C8 Substrate Binding: STRUCTURES OF COMPLEXES WITH MONTELUKAST, TROGLITAZONE, FELODIPINE, AND 9-CIS-RETINOIC ACIDCrystal Structures of Cytochrome P450 105P1 from Streptomyces avermitilis: Conformational Flexibility and Histidine Ligation StateIdentification and structural basis of the reaction catalyzed by CYP121, an essential cytochrome P450 in Mycobacterium tuberculosisP450cam Visits an Open Conformation in the Absence of Substrate ,Regio- and stereospecificity of filipin hydroxylation sites revealed by crystal structures of cytochrome P450 105P1 and 105D6 from Streptomyces avermitilis.The role of Ile87 of CYP158A2 in oxidative coupling reactionFunctional and structural characterisation of a viral cytochrome b5Detection of trans-cis flips and peptide-plane flips in protein structuresVariations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamilyMicrobial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us?Elucidation of cladofulvin biosynthesis reveals a cytochrome P450 monooxygenase required for anthraquinone dimerizationThree clusters of conformational states in p450cam reveal a multistep pathway for closing of the substrate access channel.Prioritizing orphan proteins for further study using phylogenomics and gene expression profiles in Streptomyces coelicolor.Molecular cloning and characterization of CYP80G2, a cytochrome P450 that catalyzes an intramolecular C-C phenol coupling of (S)-reticuline in magnoflorine biosynthesis, from cultured Coptis japonica cells.Streptomyces coelicolor A3(2) CYP102 protein, a novel fatty acid hydroxylase encoded as a heme domain without an N-terminal redox partnerRole of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer.Recent Structural Insights into Cytochrome P450 Function.Iron(IV)hydroxide pK(a) and the role of thiolate ligation in C-H bond activation by cytochrome P450Tandem expression in E. coli of type III PKS and P450 genes from marine Streptomyces olivaceus FXJ 7.023 gives production of phenol and indole.Structural analysis of cytochrome P450 105N1 involved in the biosynthesis of the zincophore, coelibactin.Coupling Oxygen Consumption with Hydrocarbon Oxidation in Bacterial Multicomponent Monooxygenases.Unusual properties of the cytochrome P450 superfamily.Exploiting Streptomyces coelicolor A3(2) P450s as a model for application in drug discovery.Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.Mechanism of drug-drug interactions mediated by human cytochrome P450 CYP3A4 monomerUnusual cytochrome p450 enzymes and reactions.Novel properties of P450s in Streptomyces coelicolor.Oxygen activation by cytochrome P450 monooxygenaseSubstrate binding to cytochromes P450.Cooperative properties of cytochromes P450.Characterization of a Biflaviolin Synthase CYP158A3 from Streptomyces avermitilis and Its Role in the Biosynthesis of Secondary Metabolites.Conformational plasticity and structure/function relationships in cytochromes P450.Diversity of P450 enzymes in the biosynthesis of natural productsExploitation of the Streptomyces coelicolor A3(2) genome sequence for discovery of new natural products and biosynthetic pathways.The biocatalytic repertoire of natural biaryl formation.Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
P2860
Q24648509-1AE9A36D-2828-4216-8E0A-1EA2903E8002Q24651857-ABBB6F9A-1723-4E88-A5FA-33C624F4AD5EQ24677369-57354A33-4081-40F8-BD25-580F4DAF86EBQ27649360-8BAD263E-4EBE-46AC-A9C4-AAB10FD81CDDQ27650327-AEF99284-4864-4F5B-81B5-D74704F15A7BQ27653132-218EC6F9-52EC-426F-9EA8-858994B5D6B2Q27655377-892C19C7-2C7D-4542-9F6D-EA45BE213C9AQ27660275-73B4CBB6-B39A-43B1-8892-1AA48EE87AEAQ27660445-86290C24-6D5A-4F4C-8147-650E207FC329Q27676475-78D6751B-ACB1-40CB-B049-B62F7B6ED284Q27686957-9D3BAFF5-7051-4B57-8DE9-990B59971B5FQ28265964-B1C65764-B418-4553-B994-3F8CF3D16E05Q28304165-DD959F7A-2DE6-4406-A35A-1EDCAEB32448Q28710079-789BE63B-6920-4819-83CE-122FD02A9582Q28828786-18CAEDF6-9F34-4523-B8EF-518FA59EC949Q30498059-1D6E0091-1BAE-4B2F-8955-E072265B8554Q31030494-E6E36676-DDA4-4974-8510-2FF4E940B4ACQ33317128-6DA77C20-F890-46CE-BAE5-B1BF8C75A41BQ33725278-3EFDB7F4-D4C1-4C76-A382-AA6455970A6EQ34461465-8728567D-4F3F-40D3-AF1B-BF8814D24679Q34529849-0CA58B04-E56F-42A4-BF45-35412CEDA5FBQ34987922-D35AC2C6-7240-4217-860C-0D6F65705165Q35564177-63DCC103-6AA3-4A79-8677-5207104D4078Q36197239-960A1414-5EFC-4DCE-9934-5D834983FA25Q36218556-279B5EA6-EAC6-4C52-881D-AF6F729F8A53Q36512916-CA4EABBE-11D8-4BBD-8796-23A493030696Q36545019-8747A683-B184-417D-8A85-8795EBEEBEA7Q36580605-CCE345F8-E014-45DC-A83D-BE37AF3B0308Q36590427-5DB2B42E-51EF-4946-9C12-B2049C2E77A5Q36928916-0F535B1D-9DE1-45BF-8429-D1CDA3DD3654Q36929579-D99F7A51-20A5-41A0-993B-2076AB3EE477Q37207087-7A429BFD-C66A-4899-AB0D-8B84A1285074Q37214645-6FF1F959-2B92-4CCB-80FB-CB2B4C24AD67Q37366156-158532D3-6047-4083-9187-5F62722811C5Q37685097-5C360A73-D1FC-498F-A643-3C15FD4297AEQ37743467-1D9BA383-CCC6-43A2-9226-FC6741534A06Q38028349-24E683D6-1949-4A99-85FC-8CD6CA5DF793Q38169895-260F8C36-3DAB-4C07-88F5-6900B16B216BQ38232045-85554DDB-3B8C-4F42-8654-46414ACB5FD6Q38429569-21EEC9E1-4283-4BCD-A207-863CD2E4A507
P2860
Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2
description
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2005
@ast
im März 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2005/03/25)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/03/25)
@nl
наукова стаття, опублікована в березні 2005
@uk
name
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@ast
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@en
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@nl
type
label
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@ast
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@en
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@nl
prefLabel
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@ast
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@en
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@nl
P2093
P356
P1476
Binding of two flaviolin subst ...... or A3(2) cytochrome P450 158A2
@en
P2093
Aouatef Bellamine
Bradley S. Moore
David C. Lamb
Donald Stec
F. Peter Guengerich
John A. Kalaitzis
John R. Falck
L. Manmohan Reddy
Larissa M. Podust
P304
11599–11607
P356
10.1074/JBC.M410933200
P407
P577
2005-03-25T00:00:00Z