Feb 8, 2016 · TETs are dodecameric particles of 500 kDa and they were first discovered in archaea and then identified in bacteria and eukaryotes 3, 4, 5, 6, 7. To date, three types of archaeal TETs have...

May 18, 2021 · In this study, we probed the key amino acid changes leading to the enhancement of Tet (X) function and clarified the structural characteristics and evolutionary path of Tet (X) based upon the key residue changes.

In enzymology, the turnover number (kcat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [ET] for enzymes with two or more active sites. [1] . For enzymes with a single active site, kcat is referred to as the catalytic constant. [2]

Inactivation of tetracycline antibiotics by tetracycline destructases (TDases) remains a clinical and agricultural threat. TDases can be classified as type 1 Tet (X)-like TDases and type 2...

We monitored the reaction kinetics using the intrinsic fluorescence of the tryptophan residue in position 5 of the peptide and found that all of the alkyltins analyzed are progressively degraded to dialkyl derivatives, following a pseudo-enzymatic reaction mechanism.

Kcat is turnover number, expresed as number of substrate molecules turned into product per enzyme site per minute. Km and X are both in the same units of substrate concentration. Prism will fit Kcat and Km, each with a confidence interval.

K cat is a parameter that measures the catalytic efficiency of an enzyme. The K cat value represents the number of substrate molecules an enzyme can convert into a product per unit of time when fully saturated with substrates. K cat is also referred to as the turnover number or catalytic constant.

Question: From a kinetics experiment, kcat was detetmined to be 60sec^-1. for the kinetic assay, 0.3 mL of a 0.36 mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 70,000 g/mole. assume a reaction volume of 3 mL. Calculate Vmax (uM•min^-1) for the enzyme and catalytic efficiency (in M^-1sec^-1) for the enzyme.

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