Enzymatic basis of ribosomal peptide prenylation in cyanobacteria. - Wikidata - wikimedia - TriplyDB

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

http://www.wikidata.org/entity/Q38368483

about

Structure of PatF fromProchloron didemni Analysis of an inactive cyanobactin biosynthetic gene cluster leads to discovery of new natural products from strains of the genus Microcystis Combining a Clostridial enzyme exhibiting unusual active site plasticity with a remarkably facile sigmatropic rearrangement: rapid, stereocontrolled entry into densely functionalized fluorinated phosphonates for chemical biology Aestuaramides, a natural library of cyanobactin cyclic peptides resulting from isoprene-derived Claisen rearrangements.Ribosomal route to small-molecule diversity Selectivity, directionality, and promiscuity in peptide processing from a Bacillus sp. Al Hakam cyclodehydratase.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Assessing the combinatorial potential of the RiPP cyanobactin tru pathway Recognition sequences and substrate evolution in cyanobactin biosynthesis Combinatorial biosynthesis of RiPPs: docking with marine life.The 3,4-dioxygenated 5-hydroxy-4-aryl-quinolin-2(1H)-one alkaloids. Results of 20 years of research, uncovering a new family of natural products.Cyanobactins from Cyanobacteria: Current Genetic and Chemical State of Knowledge.Metabolic model for diversity-generating biosynthesis Revealing nature's synthetic potential through the study of ribosomal natural product biosynthesis.Asymmetric Enzymatic Synthesis of Allylic Amines: A Sigmatropic Rearrangement Strategy.Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis.A Unique Tryptophan C-Prenyltransferase from the Kawaguchipeptin Biosynthetic Pathway Aromatic Claisen Rearrangements of O-prenylated tyrosine and model prenyl aryl ethers: Computational study of the role of water on acceleration of Claisen rearrangements.Molecular basis for the broad substrate selectivity of a peptide prenyltransferase.Orchestration of enzymatic processing by thiazole/oxazole-modified microcin dehydrogenases.Acceleration of an aromatic Claisen rearrangement via a designed spiroligozyme catalyst that mimics the ketosteroid isomerase catalytic dyad.Origin and variation of tunicate secondary metabolites.Understanding and applying tyrosine biochemical diversity.Mechanistic studies on the indole prenyltransferases.The structural biology of patellamide biosynthesis Prenyltransferases as key enzymes in primary and secondary metabolism.Unique marine derived cyanobacterial biosynthetic genes for chemical diversity.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.The Enzymology of Organic Transformations: A Survey of Name Reactions in Biological Systems.Mechanisms of cyanobactin biosynthesis Posttranslational isoprenylation of tryptophan in bacteria.Directing Biosynthesis: Practical Supply of Natural and Unnatural Cyanobactins.Modularity of RiPP Enzymes Enables Designed Synthesis of Decorated Peptides.Enzyme-Catalyzed Intramolecular Enantioselective Hydroalkoxylation.Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme.Recent Advances in Enzymatic Complexity Generation: Cyclization Reactions.Ribosomal Natural Products, Tailored To Fit.Enzymatic N- and C-Protection in Cyanobactin RiPP Natural Products.Parallel lives of symbionts and hosts: chemical mutualism in marine animals.Stereospecific prenylation of tryptophan by a cyanobacterial post-translational modification enzyme.

P2860

Q27678410-AF5CF0C3-38DE-423A-8DFB-BFB6584FED3D Q28482661-E951F511-4A85-4CF3-B253-23CFB24EA677 Q28833210-9CAD233D-0CE5-443A-BE87-4B19664E4355 Q31111161-8920A91E-F3AD-41C7-9DDA-F582D050232C Q34080175-CCE423A4-6706-4385-8F38-8F63CE2290DF Q34188549-4589B616-60A6-49E2-B82C-4BF450C1D74D Q34312732-F9F68C3B-7D5D-42CC-8808-84627BE30BFB Q35228563-AFDCBA45-055B-4429-A371-5183552C0B3C Q35262723-48420325-B333-4993-860B-8D4001904CDF Q35879503-5ACECE41-756E-4419-9B5A-9D3583486EC8 Q36156035-5C58025D-AD8A-4BFC-A2F3-CCA765892C41 Q36329726-7EAB80EA-C7DA-4FE4-AE70-4CC35F89663E Q36607587-6705D943-F1BD-4085-B5BA-DA30954F07CF Q36691575-61490EF0-41F0-4C84-9998-FB69FBF5AC75 Q36759133-1DB86312-AC1F-4FF5-815C-98701A3365C9 Q37338841-3ADC0B6D-45C8-4027-985E-FFEE8F8A49E5 Q37412719-953F159E-79EE-4B27-BC8C-A6350FF450C7 Q37414681-83F1BE7E-E490-4E52-82DB-0AC66E453B06 Q37493158-4A2399C4-2B08-421E-B45A-B432A7672563 Q37592315-DA574BAC-7E85-463D-84CE-3A1B71C4A7AF Q37731590-E5AEA0EA-D290-4F5C-8118-1B518C076F2A Q37974694-77E2688B-8DF8-4723-892D-5510A4047553 Q38195522-0E0E7E32-F15D-4C4C-9A35-A2C181A61001 Q38255721-D9598070-9006-4B7D-B944-062EAF170BC6 Q38280503-39F50505-1AD0-417E-A4DF-9A9532B90EA5 Q38555536-1E95F5DA-BC38-405B-87B5-EE3A0FDEB6FF Q38693793-B91E67D4-FD4C-468E-AB6D-077F7035A494 Q38751212-AE8A4DF2-4AF6-4490-95C4-D92CB739A5B1 Q38922927-48E3B6EC-F066-4D34-8351-41F83AF65E26 Q38957421-02129FB3-D0B2-4592-891C-31585387F49B Q39191891-D554DAA8-71A9-401F-A59A-BD5EF8EFA073 Q39600741-AA0C8B40-262A-4AE8-BFA6-311CE408F21F Q40747661-3F5DEBE7-88A5-4231-8632-493DC8D9721B Q42197736-7A2D28DE-62B4-4E2F-854B-DDF2F594C661 Q42556921-425D67C9-A802-4BFD-A752-EF5FF5E86952 Q47253440-82D3F4C9-E20D-43A7-9E3F-01494444E184 Q47953416-D3A0B6F8-6045-4FB7-BFB8-A2F60BC4397F Q48239692-93F50E41-B7C2-4F30-B3A5-4C96ED386F29 Q50021280-A66F006E-D9E0-4957-963F-A32A025B9836 Q51420950-DA2EDDF4-DE2B-44A7-B08E-082647AEC63D

P2860

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

http://www.wikidata.org/entity/Q38368483

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

@en

type

label

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

@en

prefLabel

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

@en

P1433

Q38368483-BAD6C3BE-7405-4E31-90B5-B66973A937E5

P1476

Q38368483-D0B80022-1852-4E31-B634-C9D96643ED99

P2093

Q38368483-102D3B86-391B-4A97-BCF9-DCC4CFFC6840

Q38368483-39511FE1-69E5-4997-9D19-F83F63D74701

Q38368483-4F9EA1C2-216E-4BC2-AE84-3CD90C8A8E5E

Q38368483-DEAA2DF1-E3CD-4387-AEE0-B98AA9E82A04

P2860

Q38368483-0031A3DB-64D8-471F-8439-FE580AFFE47B

Q38368483-02F424F6-3CB3-46CD-B6A3-5377BF47905B

Q38368483-0A489D4F-FED2-42F1-97B5-8DCF0466B12E

Q38368483-0BBBA757-2DFE-4464-99F1-5C1FFDB0667E

Q38368483-134B8F3A-EF75-4D3F-AFE3-4B03C4A56211

Q38368483-14A9C7DC-442D-4A87-B7FF-B2CB5AB2FE43

Q38368483-1FD97EAB-D4FB-46E1-99C4-638375240BCA

Q38368483-21A320D5-F3C9-4B1C-898D-4DA6684942D5

Q38368483-24FC0D1D-FFB3-49C7-BBB9-7C3AF01B8F7A

Q38368483-2AAE54F6-F926-4483-8B02-B7BBA8ED8D2C

P304

Q38368483-40415791-B3FB-4D4D-AFCB-5B73CA2F5E49

P31

Q38368483-A2DB4BF7-69E0-467A-A315-6434575ACA52

P356

Q38368483-45E17FF4-F646-4BC4-9811-361B13A1CE88

P407

Q38368483-FD73E2EB-2C66-43C4-8E3E-AA75A4FEBA22

P433

Q38368483-39F0C6E5-2FF9-4F09-ACAA-7699302B9ECB

P478

Q38368483-73D493A8-83F0-4F5A-802F-D6153F7A1B7C

P577

Q38368483-1AC45EB2-4735-49C5-90C4-AC8EA6F10BF0

P5875

Q38368483-57FEBDE8-8571-4E4C-A31E-9A31D079BED1

P698

Q38368483-95A51B16-B25B-47EF-B03B-3FF2435AF7CC

P921

Q38368483-A976650C-09E4-4FF5-8264-8F1AC54428F8

P932

Q38368483-9682B4F2-7F1C-47D9-B244-E11A8180EC7D

P356

P1433

Journal of the American Chemical Society

P1476

Enzymatic basis of ribosomal peptide prenylation in cyanobacteria.

@en

P2093

Eric W Schmidt

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

John A McIntosh

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

Mohamed S Donia

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

Satish K Nair

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

P2860

CloQ, a prenyltransferase involved in clorobiocin biosynthesis

Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products

Structure-function analysis of an enzymatic prenyl transfer reaction identifies a reaction chamber with modifiable specificity

Protein prenyltransferases

Molecular and structural basis of metabolic diversity mediated by prenyldiphosphate converting enzymes.

A global assembly line for cyanobactins

Genome-based characterization of two prenylation steps in the assembly of the stephacidin and notoamide anticancer agents in a marine-derived Aspergillus sp

Linking chemistry and genetics in the growing cyanobactin natural products family

Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides.

Lyngbyatoxin biosynthesis: sequence of biosynthetic gene cluster and identification of a novel aromatic prenyltransferase.

P304

13698-13705

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

P31

scholarly article

P356

10.1021/JA205458H

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

P407

P433

34

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

P478

133

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

P577

2011-08-04T00:00:00Z

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

P5875

51499971

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

P698

21766822

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

P921

P932

3170831

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