Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution - Wikidata - wikimedia - TriplyDB

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

http://www.wikidata.org/entity/Q27646601

about

Probing the Active Center of Benzaldehyde Lyase with Substitutions and the Pseudosubstrate Analogue Benzoylphosphonic Acid Methyl Ester †Influence of Organic Solvents on Enzymatic Asymmetric Carboligations Thiamin Diphosphate Activation in 1-Deoxy-d-xylulose 5-Phosphate Synthase: Insights into the Mechanism and Underlying Intermolecular Interactions Bifunctionality of the thiamin diphosphate cofactor: assignment of tautomeric/ionization states of the 4'-aminopyrimidine ring when various intermediates occupy the active sites during the catalysis of yeast pyruvate decarboxylase.

P2860

Q27650916-133C49E7-8E37-4BF7-8FB4-63503CCB5129 Q41818967-FF0AB929-21F0-4B4C-89E4-78B6A06BCEE7 Q42151697-F65BF5A6-D373-45A7-BD89-F9DCDD67E43B Q42164411-9EEEFE1E-EC74-4235-B92B-A5974688889E

P2860

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

http://www.wikidata.org/entity/Q27646601

description

2007 nî lūn-bûn

@nan

2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@ast

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@en

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@nl

type

label

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@ast

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@en

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@nl

prefLabel

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@ast

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@en

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@nl

P1433

Q27646601-964EEF9A-1043-4391-8FE4-837F85ACAC80

P1476

Q27646601-142AB0CE-DE6C-447A-9C62-DEDD2E788572

P2093

Q27646601-281995C7-82C9-4499-B6BC-FBB4698D35C3

Q27646601-58041D2D-7E86-4C6A-B123-FA386617B1A3

Q27646601-9AEDAB7D-F2E8-436B-A716-CDAE7ECB994C

Q27646601-D2DE1053-BDD7-4DB6-B58F-473808512AA1

Q27646601-EC36ADAD-8E42-4C90-9B4E-A53561049521

P2860

Q27646601-1BD22BF8-A106-410E-9A0B-7D4F08923BB5

Q27646601-29D2CFFB-CCC9-4B0F-8C08-9A08A6B1DADE

Q27646601-3A2EA7E9-997E-49C2-91D5-3F8AFE284254

Q27646601-497536FC-2AEB-4056-A634-E8F183AF71EE

Q27646601-4FD64CCE-D87C-4BDC-9131-D54EFB9EF9FB

Q27646601-653E87C2-AE1F-42C0-BDDE-A18A68634C67

Q27646601-98F2FA30-1418-4CA3-957D-42C2A8B0BECE

Q27646601-B6CE182C-BDEB-4414-80A6-C3B590FB8898

Q27646601-BCBBB36C-212A-435C-9059-8A8FFD6126C9

Q27646601-F92A5BC9-089B-4B17-96C6-E7C21E1ABC14

P304

Q27646601-1283703C-3BA5-4057-809D-65F797616850

P31

Q27646601-06E120F3-DDDB-44FE-92A3-9206DCD7822C

P356

Q27646601-F4414A92-3B76-472B-8EF0-2E8C7D4D2D68

P433

Q27646601-C0D22630-DADD-4853-862F-D026D3E3B2D9

P478

Q27646601-7503ACBA-6E9D-4D62-A44B-311AD409FFF8

P577

Q27646601-4E06B69B-61D5-41AE-8D13-2FB00D246443

P5875

Q27646601-1B2ECDCA-A250-4237-AA92-337CF917510F

P698

Q27646601-A541456A-87A9-4AFB-93BA-C714E62845B7

P921

Q27646601-0DF8FF72-C3DA-4688-95D6-EE9C1D127AC3

Q27646601-3CDB7ED7-67FC-4BEB-8961-4AF05CCDB797

Q27646601-95CE0CEA-3A69-43EC-9A97-10D503C8C8DF

P932

Q27646601-6F37D526-527A-4F20-A67D-65E9A3AFDDA6

P356

S1744309107028576

P1433

Acta Crystallographica Section F: Structural Biology Communications

P1476

Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 Å resolution

@en

P2093

A Marek Brzozowski

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

Andy Maraite

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

Gideon Grogan

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

Marion B Ansörge-Schumacher

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

Thomas Schmidt

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

P2860

Benzaldehyde lyase, a novel thiamine PPi-requiring enzyme, from Pseudomonas fluorescens biovar I

Coot: model-building tools for molecular graphics

Automated protein model building combined with iterative structure refinement

Refinement of macromolecular structures by the maximum-likelihood method

The CCP4 suite: programs for protein crystallography

Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog

Active site mutants of pyruvate decarboxylase from Zymomonas mobilis--a site-directed mutagenesis study of L112, I472, I476, E473, and N482.

An overview on 2-methyl-2,4-pentanediol in crystallization and in crystals of biological macromolecules.

Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens.

The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin.

P304

546-8

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

P31

scholarly article

P356

10.1107/S1744309107028576

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

P433

Pt 7

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

P478

63

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

P577

2007-07-01T00:00:00Z

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

P5875

6216789

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

P698

17620706

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

P921

condensed matter physics

structural biology

P932

2335142

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