Alkylation of rabbit muscle creatine kinase surface methionine residues inhibits enzyme activity in vitro.

ABSTRACT: Creatine kinase (CK) catalyzes the formation of phosphocreatine from adenosine triphosphate (ATP) and creatine. The highly reactive free cysteine residue in the active site of the enzyme (Cys²⁸³) is considered essential for the enzymatic activity. In previous studies we demonstrated that Cys²⁸³ is targeted by the alkylating chemical warfare agent sulfur mustard (SM) yielding a thioether with a hydroxyethylthioethyl (HETE)-moiety. In the present study, the effect of SM on rabbit muscle CK (rmCK) activity was investigated with special focus on the alkylation of Cys²⁸³ and of reactive methionine (Met) residues. For investigation of SM-alkylated amino acids in rmCK, micro liquid chromatography-electrospray ionization high-resolution tandem-mass spectrometry mea

SUBMITTER: Steinritz D 

PROVIDER: S-EPMC8448711 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature