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Mycobacterium tuberculosis Rv1916 is an Acetyl-CoA-Binding Protein.
Huang, Evelyn Yu-Wen; Kwai, Brooke X C; Bhusal, Ram Prasad; Bashiri, Ghader; Leung, Ivanhoe K H.
Afiliación
  • Huang EY; School of Chemistry and the Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 30 Flemington Rd, Parkville, VIC 3052, Australia.
  • Kwai BXC; School of Chemistry and the Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, 30 Flemington Rd, Parkville, VIC 3052, Australia.
  • Bhusal RP; School of Chemical Sciences, The University of Auckland, Private Bag 92019, Auckland, 1142, New Zealand.
  • Bashiri G; Present address: Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia.
  • Leung IKH; School of Chemical Sciences, The University of Auckland, Private Bag 92019, Auckland, 1142, New Zealand.
Chembiochem ; 24(14): e202300162, 2023 07 17.
Article en En | MEDLINE | ID: mdl-37211532
Isocitrate lyase (ICL) isoform 2 is an essential enzyme for some clinical Mycobacterium tuberculosis (Mtb) strains during infection. In the laboratory Mtb strain H37Rv, the icl2 gene encodes two distinct gene products - Rv1915 and Rv1916 - due to a frameshift mutation. This study aims to characterise these two gene products to understand their structure and function. While we were unable to produce Rv1915 recombinantly, soluble Rv1916 was obtained with sufficient yield for characterisation. Kinetic studies using UV-visible spectrophotometry and 1 H-NMR spectroscopy showed that recombinant Rv1916 does not possess isocitrate lyase activity, while waterLOGSY binding experiments demonstrated that it could bind acetyl-CoA. Finally, X-ray crystallography revealed structural similarities between Rv1916 and the C-terminal domain of ICL2. Considering the probable differences between full-length ICL2 and the gene products Rv1915 and Rv1916, care must be taken when using Mtb H37Rv as a model organism to study central carbon metabolism.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Mycobacterium tuberculosis Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Alemania
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Mycobacterium tuberculosis Idioma: En Revista: Chembiochem Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Alemania