Activation studies of the β-carbonic anhydrases from Escherichia coli with amino acids and amines.

ABSTRACT: A β-carbonic anhydrase (CA, EC 4.2.1.1) from the widespread bacterium Escherichia coli (EcoCAβ), encoded by the CynT2 gene, has been investigated for its catalytic properties and enzymatic activation by a panel of amino acids and amines. EcoCAβ showed a significant catalytic activity for the hydration of CO₂ to bicarbonate and a proton, with a kinetic constant k_cat of 5.3 × 10⁵ s^- and a Michaelis-Menten constant K_M of 12.9 mM. The most effective EcoCAβ activators were L- and D-DOPA, L-Tyr, 4-amino-Phe, serotonin and L-adrenaline, with K_As from 2.76 to 10.7 µM. L-His, 2-pyridyl-methylamine, L-Asn and L-Gln were relatively weak activators (K_As from 36.0 to 49.5 µM). D-His, L- and D-Phe, L

SUBMITTER: Nocentini A 

PROVIDER: S-EPMC7748406 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature