Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes. - Wikidata - awgldk - TriplyDB

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.

http://www.wikidata.org/entity/Q43758959

about

The use of ene adducts to study and engineer enoyl-thioester reductases Rational Control of Polyketide Extender Units by Structure-Based Engineering of a Crotonyl-CoA Carboxylase/Reductase in Antimycin Biosynthesis Screening of metagenomic and genomic libraries reveals three classes of bacterial enzymes that overcome the toxicity of acrylate.Screening and Engineering the Synthetic Potential of Carboxylating Reductases from Central Metabolism and Polyketide Biosynthesis.Structural Basis for Cyclopropanation by a Unique Enoyl-Acyl Carrier Protein Reductase A crotonyl-CoA reductase-carboxylase independent pathway for assembly of unusual alkylmalonyl-CoA polyketide synthase extender units.Stereocontrol within polyketide assembly lines.Recent advances in the biosynthesis of unusual polyketide synthase substrates.A synthetic pathway for the fixation of carbon dioxide in vitro.Oxidative Cyclization in Natural Product Biosynthesis Substrate interaction dynamics and oxygen control in the active site of thymidylate synthase ThyX.Structural basis for substrate specificity of methylsuccinyl-CoA dehydrogenase: an unusual member of the acyl-CoA dehydrogenase family.A conserved threonine prevents self-intoxication of enoyl-thioester reductases.Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex.InhA, the enoyl-thioester reductase from forms a covalent adduct during catalysis

P2860

Q27700192-4A3AD707-C70E-4512-B8D5-B1D013AEA818 Q27702125-ACE85AA1-BB60-469E-8AB4-52ADC5EA4A2E Q35171952-D9EBE53B-6C88-44A5-B2D8-47D5C6C4E2D4 Q35780235-BF6EB452-D163-4D1D-A143-7623F4C5D929 Q36348813-0AF1A4BD-046A-4823-800B-EA5CE19D7C6D Q37533520-3AC999A3-95A0-43E0-9C62-D6ACFE3C9493 Q38264057-A3638ACB-708F-4134-AA3D-F0129C8C07B5 Q38264066-1F0EADAB-87C5-4274-B2C4-6579FDA7BD42 Q38794278-FA35F182-8E6D-47CB-97B4-90F521E28DB0 Q39034361-C02C3CA4-8D07-4616-987B-5DC362477530 Q42243448-DC5DD012-2711-49F9-AEBC-9029DB57ACA9 Q47221251-F6ADCBFF-198A-4B20-8887-899E5B8D6D9E Q48144585-BFB023FD-324D-4ACB-9C48-93914FB5C474 Q52325818-52588399-BA9F-4AC8-B5AF-D1C7A2C253A2 Q58738007-24436E41-2D25-40F2-BE41-62E9BD4BEB8E

P2860

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.

http://www.wikidata.org/entity/Q43758959

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年学术文章

@wuu

2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

2013年學術文章

@zh

2013年學術文章

@zh-hant

name

Direct evidence for a covalent ene adduct intermediate in NAD

@nl

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.

@en

type

label

Direct evidence for a covalent ene adduct intermediate in NAD

@nl

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.

@en

prefLabel

Direct evidence for a covalent ene adduct intermediate in NAD

@nl

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes.

@en

P1433

Q43758959-684C7C0F-6630-4957-B62C-DF80A6CD3015

P1476

Q43758959-B643289E-12A1-408B-A7BD-BFED53CB76DB

P2093

Q43758959-57F1B998-989C-4F77-A077-1608BAA5089A

Q43758959-8B5224F0-5508-44FD-9969-A3050FE736E8

Q43758959-8F39C475-D891-4727-9C2D-9984E448C85F

Q43758959-9D6EB6E2-5100-4188-8C96-9553A30C125D

P2860

Q43758959-0FF804B2-32F5-4B06-B388-8020AB5E0024

Q43758959-1117D103-001B-4C2D-8F9C-E70C19516BCA

Q43758959-188FB20C-5644-4C84-912E-51058B5CF126

Q43758959-3A4ACF55-6471-465E-864F-711D66F82782

Q43758959-3FAE82BF-A960-4ED0-B235-6215D2525205

Q43758959-42F32F90-B79D-4941-B2FB-107A6D9D6EF2

Q43758959-4491E3F9-B208-4E3F-9E8A-C0460B91E091

Q43758959-4C1A1486-3F67-4FAD-9653-ECCF8294560F

Q43758959-58C58C13-02A9-47DA-A97A-A92125708246

Q43758959-5C7CEFF1-D0E0-48B7-A6B5-62E0F95F0447

P2888

Q43758959-697FE5A4-D0DF-4AE4-8F50-E00174B94D60

P304

Q43758959-D0C1D309-B529-4F81-894A-FB1598F302FC

P31

Q43758959-199AB4EE-B475-4B57-8058-42C6D49BA695

P356

Q43758959-5FA5BEB8-EFC5-49CC-9C7B-6A5DCD87F340

P433

Q43758959-3E3624FA-BD82-4AC1-A517-1081C54CEFBC

P478

Q43758959-75F06813-DC57-4C96-A048-26794590F4E2

P50

Q43758959-2B8F6EE3-F7DB-4BA4-8310-3401C172D56B

Q43758959-B2989407-16E2-4852-AF1E-3E18658D26DE

P577

Q43758959-CF8CD60C-FD7A-4908-93DD-7C7E09379E3F

P5875

Q43758959-598F73C9-95A5-4139-A8A9-13041CCAB911

P698

Q43758959-23A54D86-7317-40BF-89CB-DBC8C13B80AA

P356

P1433

Nature Chemical Biology

P1476

Direct evidence for a covalent ene adduct intermediate in NAD(P)H-dependent enzymes

@en

P2093

Dominik M Peter

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

Marc-Olivier Ebert

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

Patrick Kiefer

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

Raoul G Rosenthal

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

P2860

Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase

Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway

Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance

Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties

Unusual carbon fixation gives rise to diverse polyketide extender units

The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction

Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis

Protein production by auto-induction in high density shaking cultures

Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence.

The Ruegeria pomeroyi acuI gene has a role in DMSP catabolism and resembles yhdH of E. coli and other bacteria in conferring resistance to acrylate

P2888

P304

50-55

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

P31

scholarly article

P356

10.1038/NCHEMBIO.1385

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

P433

1

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

P478

10

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

P50

P577

2013-11-17T00:00:00Z

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

P5875

258635790

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

P698

24240506

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