用1H-NMR鉴定PncA的酶催化作用

IF 0.4 Q4 BIOCHEMICAL RESEARCH METHODS Journal of the Korean magnetic resonance society Pub Date : 2017-09-20 DOI:10.6564/JKMRS.2017.21.3.085
Jong-Jae Yi, Won-Je Kim, J. Rhee, Jongsoo Lim, Bong‐Jin Lee, W. Son
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引用次数: 0

摘要

Pyrazinamidase (PncA)是结核分枝杆菌的一种水解酶(水解酶),可以将底物PZA水解成活性形式pyrazoic acid (POA)。为了研究结核分枝杆菌PncA的水解反应,在PncA和PZA的不同摩尔比下监测了1D NMR谱。PncA以不同的摩尔比加入到PZA中,改变了PZA的线宽。这些结果表明,测定PncA酶活性可能作为PZA易感性的间接测量。
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Identification of Enzymatic Catalysis of PncA using 1H-NMR
Pyrazinamidase (PncA) from Mycobacterium tuberculosis is the hydrolytic enzyme (hydrolase) that can hydrolyze substrate PZA to active form pyrazoic acid (POA). To investigate hydrolytic reaction of M. tuberculosis PncA, 1D NMR spectra were monitored at various molar ratios of PncA and PZA. The line-width of PZA was changed as PncA was added into PZA with different molar ratios. These results suggested that determination of PncA enzymatic activity could potentially serve as an indirect measure of PZA susceptibility.
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Journal of the Korean magnetic resonance society
Journal of the Korean magnetic resonance society BIOCHEMICAL RESEARCH METHODS-
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