The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2). - Wikidata - wikimedia - TriplyDB

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

http://www.wikidata.org/entity/Q30831311

about

Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis Biosynthesis of the sesquiterpene antibiotic albaflavenone in Streptomyces coelicolor A3(2)Genomics of Actinobacteria: tracing the evolutionary history of an ancient phylum The 1.92-A structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems Comparison of the 1.85 A structure of CYP154A1 from Streptomyces coelicolor A3(2) with the closely related CYP154C1 and CYPs from antibiotic biosynthetic pathways Crystal Structures of Cytochrome P450 105P1 from Streptomyces avermitilis: Conformational Flexibility and Histidine Ligation State An Enlarged, Adaptable Active Site in CYP164 Family P450 Enzymes, the Sole P450 in Mycobacterium leprae The role of Ile87 of CYP158A2 in oxidative coupling reaction The structure of a novel electron-transfer ferredoxin from Rhodopseudomonas palustris HaA2 which contains a histidine residue in its iron-sulfur cluster-binding motif Structural basis for the 4'-hydroxylation of diclofenac by a microbial cytochrome P450 monooxygenase Cj1411c encodes for a cytochrome P450 involved in Campylobacter jejuni 81-176 pathogenicity Fungal cytochrome p450 monooxygenases: their distribution, structure, functions, family expansion, and evolutionary origin Microbial cytochromes P450: biodiversity and biotechnology. Where do cytochromes P450 come from, what do they do and what can they do for us?Availability of specific reductases controls the temporal activity of the cytochrome P450 complement of Streptomyces coelicolor A3(2).Streptomyces coelicolor A3(2) CYP102 protein, a novel fatty acid hydroxylase encoded as a heme domain without an N-terminal redox partner Construction and application of a functional library of cytochrome P450 monooxygenases from the filamentous fungus Aspergillus oryzae.Investigation of cytochromes P450 in myxobacteria: excavation of cytochromes P450 from the genome of Sorangium cellulosum So ce56.Integrating multi-omics analyses of Nonomuraea dietziae to reveal the role of soybean oil in [(4'-OH)MeLeu]4-CsA overproduction.Molecular identification and functional characterization of cytochrome P450 monooxygenases from the brown-rot basidiomycete Postia placenta.Identification and functional analysis of cytochrome P450 complement in Streptomyces virginiae IBL14.CYP105-diverse structures, functions and roles in an intriguing family of enzymes in Streptomyces.Mechanism of binding of prothioconazole to Mycosphaerella graminicola CYP51 differs from that of other azole antifungals Endogenous versus exogenous glucocorticoid responses to experimental bacterial sepsis.Cytochrome P450: what have we learned and what are the future issues?Structural analysis of cytochrome P450 105N1 involved in the biosynthesis of the zincophore, coelibactin.Unusual properties of the cytochrome P450 superfamily.Exploiting Streptomyces coelicolor A3(2) P450s as a model for application in drug discovery.Cytochrome P450 107U1 is required for sporulation and antibiotic production in Streptomyces coelicolor.Identification of a cyclosporine-specific P450 hydroxylase gene through targeted cytochrome P450 complement (CYPome) disruption in Sebekia benihana.Novel properties of P450s in Streptomyces coelicolor.Intestinal cytochromes P450 regulating the intestinal microbiota and its probiotic profile.Identification, characterization, and azole-binding properties of Mycobacterium smegmatis CYP164A2, a homolog of ML2088, the sole cytochrome P450 gene of Mycobacterium leprae.Structural diversity of cytochrome P450 enzyme system.Streptomyces cytochromes P450: applications in drug metabolism.Drug metabolism in microorganisms.Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.Biocatalytic conversion of avermectin to 4"-oxo-avermectin: characterization of biocatalytically active bacterial strains and of cytochrome p450 monooxygenase enzymes and their genes.Biocatalytic conversion of avermectin to 4"-oxo-avermectin: heterologous expression of the ema1 cytochrome P450 monooxygenase.Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coli Crystal Structure of Cytochrome P450 (CYP105P2) from Streptomyces peucetius and Its Conformational Changes in Response to Substrate Binding.

P2860

Q24632747-1B1BE7F4-8FE1-4324-A6F2-DA825A7A183D Q24648509-4744021E-53EE-4912-8AB1-D31ED26B053C Q24681753-AF44132D-2587-4CF8-95A8-2422D952CB5D Q27640294-5A4A3B35-9E19-4693-911A-E13F32546DFB Q27642846-F6CDF1F7-CD2E-4B46-8CCE-326385B61DEB Q27653132-5172F6C2-E069-40EF-84B4-A898A5AA8829 Q27675293-99A79460-78A1-4B2B-8932-D505F7A2B5B3 Q27676475-493886EC-A35D-40EE-BC02-151B156FA71F Q27690210-FA0AEED8-49CA-4274-8040-0B1C841A2444 Q27695727-288C2D7B-E884-4BD9-867A-7ECFB998D578 Q28533834-113D10D1-DDF2-448D-8797-E45D820BACEB Q28654898-524EBEB8-E7F1-4144-B0A9-58A17B305FE6 Q28710079-CBD3D174-6842-4A22-8656-5BC813AB83F5 Q33196401-D9F83CAD-88E3-4DAA-B0E2-D4F6541A422A Q33725278-2DEAF8D9-2852-466F-A39D-967A4A4FF228 Q33837981-2AB3549F-53E9-4F0D-9EE6-7ED50C2597B9 Q33882400-2D0200AC-3A8E-47FF-94F2-EE50663847D4 Q33908596-BF5A4F65-B2DA-4128-8C3C-A8E198B774A7 Q34027471-218AFA11-8D05-4F80-ACD4-57504B08EEE0 Q34329912-7592F7FB-ED97-466D-88AE-B9FC4FC2B8B7 Q34442348-94EA2331-AF3C-47C5-A68D-40CFA02E14CF Q34738064-D9C1F162-178E-46B6-BD8C-933E261936DD Q35093114-74E84D90-B441-411C-9AA2-6611CA702B82 Q35828009-0F8CEB7C-DBD9-415D-B240-39564B62CA22 Q36197239-B86A6223-A7BE-4ECB-86ED-3699543236E3 Q36512916-B776BE4F-F5CD-4A4C-942F-79363D670150 Q36545019-B2BFFF9C-4BA2-4009-9468-7F2946146708 Q36691841-FBBC5D18-7F73-48E4-AFAE-DE38D94036EE Q36757393-DBFBDDA3-CA62-419A-813E-76955B7CB162 Q36929579-43F56520-A6FE-49B8-BB99-42F3D40526F3 Q37106018-5C1F029E-4C79-48F4-AEC2-F9AD098AEE6A Q37115823-FE41830F-510E-44F1-AB34-A54C3EE6D458 Q37672815-A7572383-D8A8-4BEE-96B9-CE52E6355EBB Q38112197-7476F7B1-7AE5-4683-9B8A-6597B8F193F3 Q38245429-2B4585D8-D333-4798-B9C2-C2E8C07035DF Q38429569-3FBD40AE-D7F7-4B51-9FD9-2D307A74CBF3 Q39799191-B0D67F71-9843-4219-A861-BB9A7F6668C6 Q39799221-D21B8760-016A-4460-8EF6-D5CA5979A8E7 Q41710113-05223057-9E88-43A9-B5B1-7D9A6E70B45A Q41927575-C34EC795-3ADC-4B77-8930-2871694682CA

P2860

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

http://www.wikidata.org/entity/Q30831311

description

2002 nî lūn-bûn

@nan

2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

name

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@ast

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@en

type

label

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@ast

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@en

prefLabel

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@ast

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@en

P1433

Q30831311-5392A19D-EE09-4157-9324-8F0F6211C594

P1476

Q30831311-29B98BD7-FA1A-4D81-905E-3EBA622650A6

P2093

Q30831311-06DDC507-37C2-46C3-BE8B-89253120CEA8

Q30831311-1110D483-A0AC-4075-90EA-8E15F1BBE301

Q30831311-14E3DD5D-436C-4216-AC45-0A1C56573F01

Q30831311-640C9B36-98DC-433A-ABC0-BF09880FA772

Q30831311-6F098CF7-4E8C-46AD-AAEA-29CA327526DA

Q30831311-73DB8592-CC35-49B7-AC05-49B58310EE62

Q30831311-D1131694-F2F0-4451-A9C5-605209A5F6CC

Q30831311-DE9FC5A1-A1BF-4C08-B337-656FDBACE7A4

P2860

Q30831311-39F6EB8B-7ABC-412D-81FE-3FA8154294CC

Q30831311-40B11474-7168-429B-90C5-E0FEE51B02AD

Q30831311-6EDD7CAE-526A-4DCD-A725-ADC192BA3260

Q30831311-722AF669-A046-4B1D-AACA-99BF47302DE5

Q30831311-7808F8AE-F84D-433F-ADF2-CB8345F0A912

Q30831311-7CCDC26E-E401-4D49-BF15-D83736368791

Q30831311-9A9212B5-D741-4073-B08C-1F8748AFA934

Q30831311-BA3646C7-0887-4AE1-9DD7-478C03E49C14

Q30831311-BF99DC55-0EB0-480F-A3D8-5B6BB3EACFA3

Q30831311-D10ED887-A1D4-416B-B991-B060A41443BD

P304

Q30831311-D9925A95-1361-4D76-8369-AA4CBAF38ABB

P31

Q30831311-AB8D2BBB-18BF-492D-AE40-430AF452C286

P356

Q30831311-210D9240-A71E-48D1-9E5C-F47B505CC313

P407

Q30831311-A1A15FDB-8AB8-4A9F-9776-703192555728

P433

Q30831311-A57B14A3-8C61-42DB-8D58-5C188BC59098

P478

Q30831311-64EA433D-43B6-4D05-94FE-437439A340B6

P50

Q30831311-C52D01E4-5F95-4190-A4AE-37B400CCAA97

P577

Q30831311-4A186CF4-B391-4444-8B01-E08452C54AB7

P5875

Q30831311-FBDA1D07-521F-4D74-9BE0-3F7621D6C605

P698

Q30831311-6C490ECD-D26C-4347-966B-DD95FD0768CB

P356

P1433

Journal of Biological Chemistry

P1476

The cytochrome P450 complement (CYPome) of Streptomyces coelicolor A3(2).

@en

P2093

Colin J Jackson

http://www.w3.org/2001/XMLSchema#string

David C Lamb

http://www.w3.org/2001/XMLSchema#string

Diane E Kelly

http://www.w3.org/2001/XMLSchema#string

Hong-Lin Song

http://www.w3.org/2001/XMLSchema#string

Larissa M Podust

http://www.w3.org/2001/XMLSchema#string

Michael R Waterman

http://www.w3.org/2001/XMLSchema#string

Steven L Kelly

http://www.w3.org/2001/XMLSchema#string

Tove Skaug

http://www.w3.org/2001/XMLSchema#string

P2860

Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites

Structure of cytochrome P450eryF involved in erythromycin biosynthesis

Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis

AUD4, a new amplifiable element from Streptomyces lividans.

Cytochrome P450 and the individuality of species.

Forty years of genetics with Streptomyces: from in vivo through in vitro to in silico.

The molecular phylogeny and systematics of the actinomycetes.

The P450 superfamily: update on new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature.

Analysis of five tylosin biosynthetic genes from the tyllBA region of the Streptomyces fradiae genome.

Cloning, nucleotide sequence determination and expression of the genes encoding cytochrome P-450soy (soyC) and ferredoxinsoy (soyB) from Streptomyces griseus.

P304

24000-24005

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M111109200

http://www.w3.org/2001/XMLSchema#string

P407

P433

27

http://www.w3.org/2001/XMLSchema#string

P478

277

http://www.w3.org/2001/XMLSchema#string

P50

P577

2002-04-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11422347

http://www.w3.org/2001/XMLSchema#string

P698

11943767

http://www.w3.org/2001/XMLSchema#string