(Q44268080)

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Structural investigation of mutant Mycobacterium smegmatis arylamine N-acetyltransferase: a model for a naturally occurring functional polymorphism in Mycobacterium tuberculosis arylamine N-acetyltransferase.

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16 December 2019

Structural investigation of mutant Mycobacterium smegmatis arylamine N-acetyltransferase: a model for a naturally occurring functional polymorphism in Mycobacterium tuberculosis arylamine N-acetyltransferase (English)

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16 December 2019

Mycobacterium tuberculosis

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Mycobacterium smegmatis

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Mycobacterium smegmatis

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Mycobacterium smegmatis

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4

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16 December 2019

1

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16 December 2019

5

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Edith Sim

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16 December 2019

author name string

James Sandy

2

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16 December 2019

Anna Upton

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16 December 2019

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1 January 2003

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16 December 2019

Protein Expression and Purification

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16 December 2019

27

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16 December 2019

1

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16 December 2019

75-84

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16 December 2019

Genetic control of isoniazid metabolism in man

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Arylamine N-acetyltransferases - of mice, men and microorganisms

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Pharmacogenetics of the human arylamine N-acetyltransferases

1 reference

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The pharmacogenetics of NAT: structural aspects.

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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

1 reference

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Identification and functional characterization of arylamine N-acetyltransferases in eubacteria: evidence for highly selective acetylation of 5-aminosalicylic acid

1 reference

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Treatment of tuberculosis and tuberculosis infection in adults and children. American Thoracic Society and The Centers for Disease Control and Prevention

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Effect of isoniazid on the in vivo mycolic acid synthesis, cell growth, and viability of Mycobacterium tuberculosis

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Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis

1 reference

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inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis

1 reference

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inferred from DOI database lookup

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

1 reference

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Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

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

1 reference

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Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis

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Genome and MIC stability in Mycobacterium tuberculosis and indications for continuation of use of isoniazid in multidrug-resistant tuberculosis.

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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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Purification, characterization, and crystallization of an N-hydroxyarylamine O-acetyltransferase from Salmonella typhimurium.

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High-performance liquid chromatographic analysis of isoniazid and acetylisoniazid in biological fluids

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Drug metabolising N-acetyltransferase activity in human cell lines

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The CCP4 suite: programs for protein crystallography

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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

1 reference

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Structure of arylamine N-acetyltransferase reveals a catalytic triad

1 reference

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Identifiers

10.1016/S1046-5928(02)00592-2

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12509987%20AND%20SRC:MED&resulttype=core&format=json

16 December 2019

PubMed publication ID

1 reference

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PubMed publication ID

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16 December 2019

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