The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid (Q27639119)

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English	The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid	scientific article

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The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid (English)

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Mycobacterium smegmatis

object named as

Mycobacterium smegmatis

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based on heuristic

inferred from title

3

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5

object named as

Edith Sim

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author name string

James Sandy

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Adeel Mushtaq

2

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John Sinclair

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Martin Noble

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language of work or name

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publication date

10 May 2002

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Journal of Molecular Biology

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318

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4

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1071-83

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Genetic control of isoniazid metabolism in man

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The genetics and biochemistry of isoniazid resistance in mycobacterium tuberculosis.

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Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis

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Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid.

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Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

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Eubacterial arylamine N-acetyltransferases - identification and comparison of 18 members of the protein family with conserved active site cysteine, histidine and aspartate residues

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Evidence towards the role of arylamine N-acetyltransferase in Mycobacterium smegmatis and development of a specific antiserum against the homologous enzyme of Mycobacterium tuberculosis

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Structure of arylamine N-acetyltransferase reveals a catalytic triad

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Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism.

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10.1016/S0022-2836(02)00141-9

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