The Functional State of <i>Thermoplasma acidophilum</i> Pyruvate Kinase Relies on an Extra Carboxyl-Terminal Sequence.

ABSTRACT: Phylogenetic studies of the pyruvate kinase family reveal two clusters: the K⁺-dependent and -independent enzymes. Thermoplasma acidophilum pyruvate kinase belongs to the latter but possesses the conserved signature of those K⁺-dependent. Recently, we found two distinct ways for these groups to catalyze. It is interesting to elucidate how the T. acidophilum enzyme achieves its active conformation. A structural model of this enzyme revealed the presence of an extra C-terminal sequence (ECTS). To understand its role, an enzyme lacking this sequence from T. acidophilum was constructed. We then compared the kinetic parameters, far-UV CD spectra, thermal stability, molecular dynamics simulations, and oligomeric states of both the wild-type and truncate

SUBMITTER: Ramirez-Silva L 

PROVIDER: S-EPMC12428139 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature