Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis
about
Two-step Ligand Binding in a (βα)8 Barrel Enzyme: SUBSTRATE-BOUND STRUCTURES SHED NEW LIGHT ON THE CATALYTIC CYCLE OF HisAStructural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphataseA sugar isomerization reaction established on various (βα)₈-barrel scaffolds is based on substrate-assisted catalysisStructure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complexHarnessing Nature's Diversity: Discovering organophosphate bioscavenger characteristics among low molecular weight proteinsEvolution of substrate specificity in a retained enzyme driven by gene lossStructural and functional innovations in the real-time evolution of new (βα)8 barrel enzymes.Promiscuous and adaptable enzymes fill "holes" in the tetrahydrofolate pathway in Chlamydia species.Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.High-throughput screen of essential gene modules in Mycobacterium tuberculosis: a bibliometric approach.HisB from Mycobacterium tuberculosis: cloning, overexpression in Mycobacterium smegmatis, purification, crystallization and preliminary X-ray crystallographic analysisInsights into the evolution of enzyme substrate promiscuity after the discovery of (βα)₈ isomerase evolutionary intermediates from a diverse metagenome.Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosisRelated (βα)8-barrel proteins in histidine and tryptophan biosynthesis: a paradigm to study enzyme evolution.Advances In Mycobacterium Tuberculosis Therapeutics Discovery Utlizing Structural Biology.Emerging Targets in Photopharmacology.Enzyme evolution beyond gene duplication: A model for incorporating horizontal gene transferPrediction of detailed enzyme functions and identification of specificity determining residues by random forests.Catalytic Promiscuity of Ancestral Esterases and Hydroxynitrile Lyases.Long-Term Persistence of Bi-functionality Contributes to the Robustness of Microbial Life through Exaptation.Exploiting protein symmetry to design light-controllable enzyme inhibitors.Primordial-like enzymes from bacteria with reduced genomes.Stereocontrol in dinuclear triple lithium-bridged titanium(IV) complexes: solving some stereochemical mysteries.A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.Evolutionary convergence in the biosyntheses of the imidazole moieties of histidine and purines.
P2860
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P2860
Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
@ast
Bisubstrate specificity in his ...... s by active site metamorphosis
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Bisubstrate specificity in his ...... s by active site metamorphosis
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P2860
P50
P3181
P356
P1476
Bisubstrate specificity in his ...... s by active site metamorphosis
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P2093
Anne V Due
Jens Peter von Kries
P2860
P304
P3181
P356
10.1073/PNAS.1015996108
P407
P577
2011-03-01T00:00:00Z