Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis.
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Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discoveryStructural basis of substrate-binding specificity of human arylamine N-acetyltransferasesProbing the architecture of the Mycobacterium marinum arylamine N-acetyltransferase active siteStructural and Biochemical Characterization of an Active Arylamine N-Acetyltransferase Possessing a Non-canonical Cys-His-Glu Catalytic TriadPurification, crystallization and preliminary X-ray diffraction analysis of theN-acetyltransferase SAV0826 fromStaphylococcus aureusKinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosisFrom arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN)NAT1 and its homologue (MOUSE)NAT2Kinetic characterisation of arylamine N-acetyltransferase from Pseudomonas aeruginosa.What differs on the enzymatic acetylation mechanisms for arylamines and arylhydrazines substrates? A theoretical studyArylamine N-acetyltransferases: what we learn from genes and genomes.Arylamine N-acetyltransferases.Arylamine N-acetyltransferases in mycobacteria.Mycobacterium tuberculosis Arylamine N-Acetyltransferase Acetylates and Thus Inactivates para-Aminosalicylic AcidPharmacogenetics in reproductive and perinatal medicine.Crystal structure of arylamine N-acetyltransferases: insights into the mechanisms of action and substrate selectivity.Arylamine N-acetyltransferases: a structural perspective.Structural and functional characterization of an arylamine N-acetyltransferase from the pathogen Mycobacterium abscessus: differences from other mycobacterial isoforms and implications for selective inhibition.Investigation of the catalytic triad of arylamine N-acetyltransferases: essential residues required for acetyl transfer to arylamines.Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.Insight into the structure of Mesorhizobium loti arylamine N-acetyltransferase 2 (MLNAT2): a biochemical and computational study.
P2860
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P2860
Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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name
Binding of the anti-tubercular ...... from Mycobacterium smegmatis.
@en
Binding of the anti-tubercular ...... from Mycobacterium smegmatis.
@nl
type
label
Binding of the anti-tubercular ...... from Mycobacterium smegmatis.
@en
Binding of the anti-tubercular ...... from Mycobacterium smegmatis.
@nl
prefLabel
Binding of the anti-tubercular ...... from Mycobacterium smegmatis.
@en
Binding of the anti-tubercular ...... from Mycobacterium smegmatis.
@nl
P2860
P50
P356
P1433
P1476
Binding of the anti-tubercular ...... n from Mycobacterium smegmatis
@en
P2093
James Sandy
Simon Holton
P2860
P304
P356
10.1110/PS.041163505
P577
2005-03-01T00:00:00Z