Discussion
Efficiency of enzyme can be better measured in terms of :
Answer: D
Enzyme efficiency is best measured by \(k_{cat}/K_{m}\), the specificity constant.
\(K_{m}\) reflects how much substrate is needed for half-maximal rate, and \(k_{cat}\) is the turnover number, the number of substrate molecules converted per active site per second. Their ratio is the apparent second-order rate constant at low substrate concentration and measures both binding and catalysis together. Its upper limit is the diffusion rate, about \(10^{8}\) to \(10^{9}\) per molar per second, reached by 'catalytically perfect' enzymes such as triose phosphate isomerase.
\(K_{m}\) or \(k_{cat}\) alone captures only one side of performance, and \(K_{m}/V_{max}\) is the slope of a Lineweaver-Burk plot, not a measure of efficiency.
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