Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate.
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Differential substrate specificity and kinetic behavior of Escherichia coli YfdW and Oxalobacter formigenes formyl coenzyme A transferaseThe crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. Implications for its catalytic and regulatory mechanismMolecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylaseThe structures of pyruvate oxidase fromAerococcus viridanswith cofactors and with a reaction intermediate reveal the flexibility of the active-site tunnel for catalysisReinvestigation of the catalytic mechanism of formyl-CoA transferase, a class III CoA-transferaseNew insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coliPerturbation 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)YfdW and YfdU are required for oxalate-induced acid tolerance in Escherichia coli K-12.Acetohydroxyacid synthases: evolution, structure, and function.The oxalyl-CoA synthetase-regulated oxalate and its distinct effects on resistance to bacterial blight and aluminium toxicity in rice.Local Alignment of Ligand Binding Sites in Proteins for Polypharmacology and Drug Repositioning.Comprehensive understanding of acetohydroxyacid synthase inhibition by different herbicide families.Properties of Intermediates in the Catalytic Cycle of Oxalate Oxidoreductase and Its Suicide Inactivation by Pyruvate.Crystal structure of a ring-cleaving cyclohexane-1,2-dione hydrolase, a novel member of the thiamine diphosphate enzyme family.Protein families reflect the metabolic diversity of organisms and provide support for functional prediction.Oxalate consumption by lactobacilli: evaluation of oxalyl-CoA decarboxylase and formyl-CoA transferase activity in Lactobacillus acidophilus.A previously unknown oxalyl-CoA synthetase is important for oxalate catabolism in Arabidopsis.
P2860
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P2860
Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate.
description
2005 nî lūn-bûn
@nan
2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
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2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
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2005年學術文章
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name
Structural basis for activatio ...... lase by adenosine diphosphate.
@ast
Structural basis for activatio ...... lase by adenosine diphosphate.
@en
type
label
Structural basis for activatio ...... lase by adenosine diphosphate.
@ast
Structural basis for activatio ...... lase by adenosine diphosphate.
@en
prefLabel
Structural basis for activatio ...... lase by adenosine diphosphate.
@ast
Structural basis for activatio ...... lase by adenosine diphosphate.
@en
P2093
P2860
P356
P1476
Structural basis for activatio ...... lase by adenosine diphosphate.
@en
P2093
Catrine L Berthold
Nigel G J Richards
Patricia Moussatche
P2860
P304
41645-41654
P356
10.1074/JBC.M509921200
P407
P577
2005-10-10T00:00:00Z