Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction
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Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylasePerturbation of the Monomer–Monomer Interfaces of the Benzoylformate Decarboxylase TetramerA dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (α-ketoglutarate decarboxylase)Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae.The Thiamine diphosphate dependent Enzyme Engineering Database: a tool for the systematic analysis of sequence and structure relations.A bio-catalytic approach to aliphatic ketonesProtein engineering for metabolic engineering: current and next-generation tools.Saturated mutagenesis of ketoisovalerate decarboxylase V461 enabled specific synthesis of 1-pentanol via the ketoacid elongation cycle.Integrative genomic mining for enzyme function to enable engineering of a non-natural biosynthetic pathway.Branched-chain 2-keto acid decarboxylases derived from Psychrobacter.Computational evaluation of factors governing catalytic 2-keto acid decarboxylation.Engineering nonphosphorylative metabolism to generate lignocellulose-derived products.S-Selective Mixed Carboligation by Structure-Based Design of the Pyruvate Decarboxylase from Acetobacter pasteurianus
P2860
Q27653410-F221B171-DE74-4ECB-BB3F-810FC1FBA5D9Q27684437-5F2B3FF8-3C3A-4AB3-A32D-A9A508A8CF66Q27687388-4D8F7E9D-4E59-4FC7-9A04-E65EDEB75DBDQ27935077-CF4E1C65-5EC1-4365-A199-8EA9C0F3C0A6Q33528169-42B3BB99-7502-4397-8661-86429863BC56Q35825008-D6722E8B-9202-49B6-8A14-338EBBE70133Q38099295-1D0A7294-C8ED-482A-ADCC-F3681BEE232BQ41201852-B5607D24-66F7-40B4-9990-7A75F2683651Q42645533-746DFFE0-2FA6-4CA8-A80C-2B8935F71260Q43729959-BA195F5D-D2A6-48D7-8A90-C8E09216C4C3Q47761105-A9A3F2E6-FB6D-4648-80E1-FD2B5A83F734Q51532487-9042BF9C-A1D8-47E0-8582-8C3E5966F8A6Q58943216-E9959B31-4187-4B1C-AFA7-9FF32B5E7986
P2860
Structure of the branched-chain keto acid decarboxylase (KdcA) from Lactococcus lactis provides insights into the structural basis for the chemoselective and enantioselective carboligation reaction
description
2007 nî lūn-bûn
@nan
2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի դեկտեմբերին 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 branched-chai ...... lective carboligation reaction
@ast
Structure of the branched-chai ...... lective carboligation reaction
@en
Structure of the branched-chai ...... lective carboligation reaction
@nl
type
label
Structure of the branched-chai ...... lective carboligation reaction
@ast
Structure of the branched-chai ...... lective carboligation reaction
@en
Structure of the branched-chai ...... lective carboligation reaction
@nl
prefLabel
Structure of the branched-chai ...... lective carboligation reaction
@ast
Structure of the branched-chai ...... lective carboligation reaction
@en
Structure of the branched-chai ...... lective carboligation reaction
@nl
P2093
P50
P1476
Structure of the branched-chai ...... lective carboligation reaction
@en
P2093
Catrine L Berthold
Martin D Wood
Martina Pohl
P304
P356
10.1107/S0907444907050433
P577
2007-12-01T00:00:00Z