lab last year, biochemistry students stndi at germ acid phosphatase, which has t
ID: 1016688 • Letter: L
Question
lab last year, biochemistry students stndi at germ acid phosphatase, which has the E ber 3.132. This enzyme mumb has recentty purified from Arabidopsis thaliana and characterized Here are some of the im findings wh C: KM-0.703 mM; turnover number (ka)-1 61.9 has recently been zl e ext acterized. Here are some of the important en studied at pH = 4.50 and T-370 : molecular weight = 54,200 Daltons. Answer he following questions using these values a Given the unts of the turnover mumber, is this an apparent first or second order reaction under these conditions? (1 pt) What is the catalytic efficiency of this enzyme (2 pts)? Given your answer in "b, is this enzyme near the diffusion-controlled limin (1 pt) d. What is the value of AG for the enzyme catalyzed reaction at 37.0 C? (Please use a transmission coefficient value of0.75)04 pts) e. The uncatalyzed rate constant (wa) for the hydrolysis of phosphate monoesters has been reported to be 2.0 × 10-20 sec, If this is accurate, what is the rate enhancement provided by the acid phosphatase? 2 pts) E Given this value of rate enhancement what is the value of AAG (2 pts)Explanation / Answer
Michaelis-Menten kinetics describes the kinetics of many enzymes. It is named for Leonor Michaelis and Maud Menten. This kinetic model is valid only when the concentration of enzyme is much less than the concentration of substrate
CATALAYTIC EFFICIENCY
catalaytic effeciency is nothing but ration of f kcat /Km
catalytic effeciency =161.9/0.703
catalytic effeciency =230.3mm/sec-1
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