CloQ, a prenyltransferase involved in clorobiocin biosynthesis - Test2 - elhamkhani - TriplyDB

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

http://www.wikidata.org/entity/Q24553703

about

Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria Structure-Based Engineering Increased the Catalytic Turnover Rate of a Novel Phenazine Prenyltransferase CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis An enzyme catalyzing O-prenylation of the glucose moiety of fusicoccin A, a diterpene glucoside produced by the fungus Phomopsis amygdali Relaxed specificity in aromatic prenyltransferases Unusual N-prenylation in diazepinomicin biosynthesis: the farnesylation of a benzodiazepine substrate is catalyzed by a new member of the ABBA prenyltransferase superfamily Evolutionary relationships of microbial aromatic prenyltransferases.The ABBA family of aromatic prenyltransferases: broadening natural product diversity The biosynthetic genes for prenylated phenazines are located at two different chromosomal loci of Streptomyces cinnamonensis DSM 1042.Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp Reverse prenyltransferase in the biosynthesis of fumigaclavine C in Aspergillus fumigatus: gene expression, purification, and characterization of fumigaclavine C synthase FGAPT1.Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid.Comparative analysis of hapalindole, ambiguine and welwitindolinone gene clusters and reconstitution of indole-isonitrile biosynthesis from cyanobacteria Diversity of ABBA Prenyltransferases in Marine Streptomyces sp. CNQ-509: Promiscuous Enzymes for the Biosynthesis of Mixed Terpenoid Compounds Structural basis for non-genuine phenolic acceptor substrate specificity of Streptomyces roseochromogenes prenyltransferase CloQ from the ABBA/PT-barrel superfamily Unified biogenesis of ambiguine, fischerindole, hapalindole and welwitindolinone: identification of a monogeranylated indolenine as a cryptic common biosynthetic intermediate by an unusual magnesium-dependent aromatic prenyltransferase Antimicrobial and DNA gyrase-inhibitory activities of novel clorobiocin derivatives produced by mutasynthesis.Characterization of cyclo-acetoacetyl-L-tryptophan dimethylallyltransferase in cyclopiazonic acid biosynthesis: substrate promiscuity and site directed mutagenesis studies.Ergot alkaloids: structure diversity, biosynthetic gene clusters and functional proof of biosynthetic genes.Structural and functional dissection of aminocoumarin antibiotic biosynthesis: a review.Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.Prenyltransferases as key enzymes in primary and secondary metabolism.Molecular analysis of a 4-dimethylallyltryptophan synthase from Malbranchea aurantiaca.Biosynthetic studies on terpenoids produced by Streptomyces.A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates.A new group of aromatic prenyltransferases in fungi, catalyzing a 2,7-dihydroxynaphthalene 3-dimethylallyl-transferase reaction.Two transcription factors, CabA and CabR, are independently involved in multilevel regulation of the biosynthetic gene cluster encoding the novel aminocoumarin, cacibiocin.Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes.Homogeneous purification and characterization of LePGT1--a membrane-bound aromatic substrate prenyltransferase involved in secondary metabolism of Lithospermum erythrorhizon.Bioactive compounds from marine actinomycetes.Catalytic mechanism of aromatic prenylation by NphB.Adenylate-forming enzymes of rubradirin biosynthesis: RubC1 is a bifunctional enzyme with aminocoumarin acyl ligase and tyrosine-activating domains.A gene cluster for prenylated naphthoquinone and prenylated phenazine biosynthesis in Streptomyces cinnamonensis DSM 1042.Functional analysis of a prenyltransferase gene (paxD) in the paxilline biosynthetic gene cluster.Aromatic prenylation in phenazine biosynthesis: dihydrophenazine-1-carboxylate dimethylallyltransferase from Streptomyces anulatus.NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids.Metabolic engineering of aminocoumarins: inactivation of the methyltransferase gene cloP and generation of new clorobiocin derivatives in a heterologous host.Acyl transfer in clorobiocin biosynthesis: involvement of several proteins in the transfer of the pyrrole-2-carboxyl moiety to the deoxysugar.

P2860

Q24608866-7FA81FAB-CF5D-4748-9898-89D0F9818056 Q27657177-AED715F3-C4CD-4523-BF65-84589A76B2C5 Q27674945-5B0FAE62-8805-4362-ABC2-CB8E24261E9B Q28207717-5F557C7D-F3EA-4D66-8F67-6D045DD2E7B5 Q28258411-6DAC0362-4F02-4FA4-AC6E-EB4706B9C8E8 Q28291354-0E81C863-5499-471F-A276-4314467FAAF4 Q28537964-45B796F6-4B9E-4E38-BF88-28E71734E1DF Q30155416-8204576E-3493-410C-92E3-01A579C2F1D3 Q33322675-0C562D13-133A-422A-9508-8C9311B8EF5D Q33826785-852CF369-72CE-429F-8E20-6C617087260C Q33846415-7AA91CDD-92B3-42EF-9ED5-8320C69E6C41 Q34132115-319706A5-38CA-4861-B0EE-935851705EE9 Q34482368-EB454984-AA53-40DB-AB3A-51B96D19D20D Q34977673-DA63E908-A973-4FDE-B09D-DE19E1987FDD Q35242636-1427CF9C-C443-47AE-A20D-A77C1E0900E9 Q35867293-6776C208-0505-4CAC-873F-B9EEAFA637DB Q36327019-481D8E30-1888-4ABB-B640-C5A90F405CD8 Q36484013-991D4BD4-E673-48D1-A7C9-46B5FB94E56F Q37120952-6C6F48BF-F02A-4A4E-82E9-925F7F7B6AD0 Q37439644-9B0A6789-912A-47E6-8680-BD0EBD0449EC Q37824132-2124FBE8-9CFA-4C2B-B6CC-FDDFFE92F9E5 Q38014319-DE1F41CB-8D84-4F39-9A1E-33B2C8806D33 Q38368483-0BBBA757-2DFE-4464-99F1-5C1FFDB0667E Q38555536-B2956370-20B8-4CB3-B25C-1FD4B2B6F6DB Q38868226-AF50B46D-27BD-4DB6-BC2A-A6E163361426 Q39135500-B9270203-4131-4863-A9A6-DC13A9C9D37F Q40227771-63F37F51-6F94-4F22-9DE1-CA67DC4623C4 Q40798129-B8FACBC0-0862-434A-9022-60A5B02F7FA9 Q40882702-0DAA35BB-F8EA-46EF-9CC2-AFC56787F0C3 Q41916722-49FC87BC-760C-416C-9F01-4E387587BAF8 Q42009261-839756F2-8CF6-4CD7-ACA6-A70B30B302EF Q42412549-A7BA572A-7747-4FA9-B998-E8BDD866067F Q42563815-B342E2A9-10E5-438E-96B6-8EB8D77D8B19 Q42595591-6E102CBB-896E-410E-89FA-69E357AED09E Q42603452-AD7BC968-0DF6-4497-A3AF-62E759AF59F8 Q42712318-761ACFDB-7E71-4225-ADD5-72B62572CC85 Q42982789-A8EB9114-996B-48FF-BEF2-DFD97DE20637 Q44130225-9E180905-C2E5-4B04-900F-FEC217685AD3 Q46565627-6B8F3B96-D8DF-45F2-8863-05520C8FC863 Q46795511-7AE8D4ED-A20F-4C8A-ADE7-DE0220645DD5

P2860

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

http://www.wikidata.org/entity/Q24553703

description

2003 nî lūn-bûn

@nan

2003 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի մարտին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@ast

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@en

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@nl

type

label

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@ast

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@en

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@nl

prefLabel

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@ast

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@en

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@nl

P1433

Q24553703-BEFDEF9A-8342-4412-88A7-5482CDD7D1D9

P1476

Q24553703-7CF4622D-78EA-402F-93CA-176A39C9CE77

P2093

Q24553703-166BDE55-0373-4FB0-A3CF-6620F6234A7F

Q24553703-3B78991E-FB99-4260-8FBB-033334A8EF25

Q24553703-58CC7D99-F470-4D7E-8773-10153C1849B4

Q24553703-B22D481A-E0D0-4E43-9D5B-4AFB29A0DC2E

Q24553703-D2125F8F-0DDF-4895-9E42-4C009E899C9A

Q24553703-EE32D057-E3AC-4A58-A842-2A9EC3A42447

P2860

Q24553703-0C666D29-AC1A-43D5-ABF1-A6425C64646C

Q24553703-15741B78-681E-4380-BD19-45DA44D21B3C

Q24553703-173A92A7-A91F-4AE7-BB15-61C394ED1BBD

Q24553703-22D8FBEE-1089-40D4-8EDB-6D7C6A308155

Q24553703-3E9D12FC-D49B-49FA-92E1-08523E0E7043

Q24553703-3F4F7C4A-2D8A-4A7B-9A0B-0298C668371C

Q24553703-413CFFFF-95C4-43A5-8A13-5E13F681DAB3

Q24553703-4E0858F6-B929-49AC-BF12-2542C64F33E4

Q24553703-5B3BBECC-D850-4580-96C2-E9CBCC4D7351

Q24553703-6413C072-2207-4E6F-9ACF-76B147731B62

P304

Q24553703-A6993F57-1556-42FA-B39D-16478C047273

P31

Q24553703-AABF52B0-B6ED-4EF0-A7BE-F2E689B43B95

P356

Q24553703-E2FC9D7F-8EF6-427F-9FCA-D38A538CD6DA

P407

Q24553703-E54B4A0C-7F21-4FE6-B94B-8764F907F3C0

P433

Q24553703-46F785F5-A6E4-4F6E-BFD2-402DE29C7F32

P478

Q24553703-B70FD33D-A865-45BB-A442-654480B68BC7

P50

Q24553703-721EBD93-23F2-4E83-9A1E-D933FF0C7BA4

P577

Q24553703-D288CD1D-E3CF-4B86-9AFB-83F626AF8CB1

P5875

Q24553703-A0C05AFE-3A18-40E9-B592-72C9486B5862

P698

Q24553703-41183334-9FC4-4B46-A298-B91EA44E0970

P921

Q24553703-0CE315B4-96D7-4AA9-96D9-CE38A10BBB66

Q24553703-2F612611-50E1-42A9-8078-EE27F969D914

Q24553703-87301830-2188-4F20-BBC2-B8DDE641E83B

P932

Q24553703-390CFA22-EB15-447E-BB00-1385CD77360B

P356

PNAS.0337708100

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

@en

P2093

Bernd Kammerer

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

Christopher T Walsh

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

Emmanuel Wemakor

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

Florence Pojer

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

Huawei Chen

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

Shu-Ming Li

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

P2860

Identification of the novobiocin biosynthetic gene cluster of Streptomyces spheroides NCIB 11891

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli.

Coumarin formation in novobiocin biosynthesis: beta-hydroxylation of the aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI

The search for synonyms among streptomycetes by using SDS-PAGE of whole-cell proteins. Emendation of the species Streptomyces aurantiacus, Streptomyces cacaoi subsp. cacaoi, Streptomyces caeruleus and Streptomyces violaceus

Isolation and functional analysis of homogentisate phytyltransferase from Synechocystis sp. PCC 6803 and Arabidopsis

Ubiquinone biosynthesis in microorganisms

Identification of the coumermycin A(1) biosynthetic gene cluster of Streptomyces rishiriensis DSM 40489

Molecular cloning and sequence analysis of the clorobiocin biosynthetic gene cluster: new insights into the biosynthesis of aminocoumarin antibiotics.

P304

2316-2321

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

P31

scholarly article

P356

10.1073/PNAS.0337708100

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

P407

P433

5

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

P478

100

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

P50

P577

2003-03-01T00:00:00Z

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

P5875

10871478

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

P698

12618544

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

P921

3-dimethylallyl-4-hydroxybenzoic acid

3-dimethylallyl-4-hydroxyphenylpyruvic acid

3-dimethylallyl-4-hydroxyphenylpyruvate(1-)

P932

151338

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