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谷氨酸脱氢酶中组氨酸残基与焦碳酸二乙酯的反应。

The reaction of a histidine residue in glutamate dehydrogenase with diethyl pyrocarbonate.

作者信息

Wallis R B, Holbrook J J

出版信息

Biochem J. 1973 May;133(1):183-7. doi: 10.1042/bj1330183.

Abstract
  1. One mol of diethyl pyrocarbonate will react with one mol of glutamate dehydrogenase polypeptide chains to form one mol of N(1)-carbethoxyhistidine. Reaction is prevented by NADH. 2. The 1:1 complex has an increased specific activity (1.4-2.0-fold). 3. The reason for the activation is discussed. The results are not consistent with NADH dissociation from the enzyme-glutamate-NADH complex being rate-limiting in the steady state measured. 4. The effects of modification on the properties of the enzyme were investigated. The effects of GTP and NAD(+) on the enzyme activity are unaltered by activation. NADH binding is unaltered and there is no apparent change in the molecular weight. However, the activated enzyme can still be further activated by ADP. K(s) for ADP is decreased fivefold.
摘要
  1. 一摩尔焦碳酸二乙酯会与一摩尔谷氨酸脱氢酶多肽链反应,形成一摩尔N(1)-乙氧羰基组氨酸。NADH可阻止该反应。2. 1:1复合物的比活性增加(1.4至2.0倍)。3. 讨论了激活的原因。结果与在稳态测量中NADH从酶-谷氨酸-NADH复合物解离作为限速因素不一致。4. 研究了修饰对酶性质的影响。GTP和NAD(+)对酶活性的影响不受激活的改变。NADH结合未改变,分子量也无明显变化。然而,活化酶仍可被ADP进一步激活。ADP的K(s)降低了五倍。

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