Chymotrypsin turnover number

Turnover numbers of enzymes vary from <1 to 106 s . Trypsin, chymotrypsin, and many intracellular... 

The turnover number (kCM) and the Michaelis constant (Km) as a function of pH for the hydrolysis of /V-acetyl-[ -tryptophanamide by chymotrypsin at 25°C. The decrease in fccat as the pH is lowered between 8 and 6 probably reflects the protonation of His 57. The increase in Km above pH 9 probably reflects the deprotonation of He 16, which results in the rotation of Gly 193 out of the substratebinding site. 

In addition, as is shown in Table 13, the deacylation which is represented in kd is increased by a factor of more than 103 in poly(PHA-IM-am), compared with poly(PHA-am). As is observed in the deacylation which is catalysed by imidazole moiety in the case of a-chymotrypsin, the catalysis by imidazole moiety in the deacylation of the acylated hydroxamic acid is considered. The turnover number, turnover hi poly(PHA-IM-am) is also high. The deacylation rate of poly(PHA-IM-am)... 

Which of the following statements is correct The turnover number for chymotrypsin is... 

The parameter is also referred to as the turnover number. It is the number of substrate molecules converted to product in a given time on a single-enzyme molecule when the enzyme is saturated with substrate (i.e all the active sites on the enzyme are occupied. (S) Km). For example, the turnover number for the decomposition of hydrogen-peroxide. H2O1. by the enzyme catalase is 40 x 10 s". That is, 40 million molecules of are decomposed every second on a single-enzyme molecule saturated with HiOi. The constant (mol/dm ) is called the Michaetis constant and for simple systems is a measure of the attraction of the enzyme for its subspate, so it s also called the affinity constant. The Michael is constant, /(m, for the decomposition of HiOj discussed earlier is 1.1 M, while that for chymotrypsin is 0.1 M. ... 

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