影响嗜热链球菌乳酸脱氢酶活性的因素。
Factors affecting the activity of the lactate dehydrognease of Streptococcus cremoris.
作者信息
Jonas H A, Anders R F, Jago G R
出版信息
J Bacteriol. 1972 Aug;111(2):397-403. doi: 10.1128/jb.111.2.397-403.1972.
Abstract
Studies with partially purified extracts of the nicotinamide adenine dinucleotide-linked l(+)-lactate dehydrogenase of Streptococcus cremoris US3 showed that fructose-1,6-diphosphate (FDP) was essential for the catalytic reduction of pyruvate in the pH range 5.0 to 7.0, outside of which the organism does not grow. In the absence of FDP, enzyme activity was observed only in the region of pH 8.0. The optimal pH for the oxidation of lactate was approximately 8.0 in the presence and absence of FDP. The FDP-activated enzyme was markedly inhibited by inorganic phosphate. The enzyme lost activity on standing at 5 C in alkaline triethanolamine, was quite stable at pH 6.0 to 6.5, and underwent irreversible denaturation below pH 5.0. Inorganic phosphate or FDP increased the stability of the enzyme in alkaline buffers. Some distinguishing properties of individual lactate dehydrogenases, activated by FDP, are discussed.
摘要
对嗜热链球菌US3中烟酰胺腺嘌呤二核苷酸连接的l(+)-乳酸脱氢酶部分纯化提取物的研究表明，在pH值5.0至7.0范围内，果糖-1,6-二磷酸（FDP）对于丙酮酸的催化还原至关重要，在此范围之外该生物体无法生长。在没有FDP的情况下，仅在pH 8.0区域观察到酶活性。无论有无FDP，乳酸氧化的最佳pH值约为8.0。FDP激活的酶受到无机磷酸盐的显著抑制。该酶在碱性三乙醇胺中于5℃放置时会失去活性，在pH 6.0至6.5时相当稳定，在pH 5.0以下会发生不可逆变性。无机磷酸盐或FDP可提高该酶在碱性缓冲液中的稳定性。讨论了由FDP激活的各个乳酸脱氢酶的一些独特性质。
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