Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily

Autor: Babbitt, Patricia, Casey, AK, Hicks, MA, Johnson, JL, Babbitt, PC, Frantom, PA

Publikováno v: Babbitt, Patricia; Casey, AK; Hicks, MA; Johnson, JL; Babbitt, PC; & Frantom, PA. (2014). Mechanistic and bioinformatic investigation of a conserved active site helix in α-isopropylmalate synthase from mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/8v93m66z

The characterization of functionally diverse enzyme superfamilies provides the opportunity to identify evolutionarily conserved catalytic strategies, as well as amino acid substitutions responsible for the evolution of new functions or specificities.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::925f00f1b3a88b67691c745d594ce028
http://www.escholarship.org/uc/item/8v93m66z

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The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.

Autor: Gogar RK; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama, USA., Chhikara N; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama, USA., Vo M; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama, USA., Gilbert NC; Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana, USA., Dunkle JA; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama, USA. Electronic address: jadunkle@ua.edu., Frantom PA; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama, USA. Electronic address: pfrantom@ua.edu.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2024 Sep; Vol. 300 (9), pp. 107641. Date of Electronic Publication: 2024 Aug 08.

In Vitro and In Silico Explorations of the Protein Conformational Changes of Corynebacterium glutamicum MshA, a Model Retaining GT-B Glycosyltransferase.

Autor: Hassan BA; Department of Chemistry, Wesleyan University, Middletown, Connecticut 06459, United States., Milicaj J; Department of Chemistry, Wesleyan University, Middletown, Connecticut 06459, United States., Tyson M; Department of Chemistry, Wesleyan University, Middletown, Connecticut 06459, United States., Karki R; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama 35487, United States., Sham YY; Bioinformatics and Computational Biology Program, University of Minnesota, Minneapolis, Minnesota 55455, United States.; Department of Integrative Biology and Physiology, Medical School, University of Minnesota, Minneapolis, Minnesota 55455, United States., Frantom PA; Department of Chemistry & Biochemistry, The University of Alabama, Tuscaloosa, Alabama 35487, United States., Taylor EA; Department of Chemistry, Wesleyan University, Middletown, Connecticut 06459, United States.

Publikováno v: Biochemistry [Biochemistry] 2024 Apr 02; Vol. 63 (7), pp. 939-951. Date of Electronic Publication: 2024 Mar 20.