牛晶状体醛脱氢酶。动力学与机制。
Bovine lens aldehyde dehydrogenase. Kinetics and mechanism.
作者信息
Ting H H, Crabbe M J
出版信息
Biochem J. 1983 Nov 1;215(2):361-8. doi: 10.1042/bj2150361.
Abstract
Bovine lens cytoplasmic aldehyde dehydrogenase exhibits Michaelis-Menten kinetics with acetaldehyde, glyceraldehyde 3-phosphate, p-nitrobenzaldehyde, propionaldehyde, glycolaldehyde, glyceraldehyde, phenylacetylaldehyde and succinic semialdehyde as substrates. The enzyme was also active with malondialdehyde, and exhibited an esterase activity. Steady-state kinetic analyses show that the enzyme exhibits a compulsory-ordered ternary-complex mechanism with NAD+ binding before acetaldehyde. The enzyme was inhibited by disulfiram and by p-chloromercuribenzoate, and studies with with mercaptans indicated the involvement of thiol groups in catalysis.
摘要
牛晶状体细胞质醛脱氢酶以乙醛、3-磷酸甘油醛、对硝基苯甲醛、丙醛、乙醇醛、甘油醛、苯乙酰醛和琥珀酸半醛为底物时呈现米氏动力学。该酶对丙二醛也有活性，并表现出酯酶活性。稳态动力学分析表明，该酶呈现一种强制有序的三元复合物机制，NAD⁺在乙醛之前结合。该酶受到双硫仑和对氯汞苯甲酸的抑制，对硫醇的研究表明硫醇基团参与催化作用。
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