Biochemical and structural characterization of tyrosine aminotransferase suggests broad substrate specificity and a two-state folding mechanism in Leishmania donovani.

ABSTRACT: Tyrosine aminotransferase (TAT) is an aminotransferase with broad substrate specificity that catalyzes the transamination of aromatic amino acids in Leishmania donovani and plays a crucial role in the survival and pathogenicity of the parasite. In this study, we have biochemically characterized tyrosine aminotransferase from Leishmania donovani using in vitro and in silico techniques. Leishmania donovani tyrosine aminotransferase (LdTAT) was cloned into the pET28a(+) vector and expressed in the BL21 strain of Escherichia coli. The Ni-NTA-purified protein was then characterized biochemically, and its various kinetic parameters were investigated. The apparent K_m value for the tyrosine-pyruvate pair was determined to be 3.5 ± 0.9 mm, and V_max was analyzed to be at 11.7 ±

SUBMITTER: Sasidharan S 

PROVIDER: S-EPMC6768288 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature