Kistler W S, Lin E C
J Bacteriol. 1972 Oct;112(1):539-47. doi: 10.1128/jb.112.1.539-547.1972.
The anaerobic l-alpha-glycerophosphate (l-alpha-GP) dehydrogenase of Escherichia coli was purified approximately 40-fold. The activity of the dehydrogenase, although not affected by the addition of pyridine nucleotides, was stimulated three- to fourfold by flavine adenine dinucleotide (K(m) about 10(-7)m) and up to 10-fold by flavine mononucleotide (K(m) about 10(-4)m). Maximal activity of the enzyme was found only in the combined presence of saturating concentrations of both flavines (stimulation by a factor of 10 to 15). The dependence of the rate of the reaction on the concentration of l-alpha-GP was complex in the presence of both flavines, but in the presence of flavine adenine dinucleotide alone the kinetics were of the Michaelis-Menten type with the K(m) for l-alpha-GP being about 10(-4)m. The product of the reaction was identified as dihydroxyacetone phosphate, and the molecular weight of the dehydrogenase was estimated to be 80,000 +/- 10,000. Phenazine methosulfate, menadione and ferricyanide served as artificial acceptors for the dehydrogenase. The enzyme was sensitive to iodoacetate, p-chloromercuribenzoate, and N-ethymaleimide.
大肠杆菌的厌氧L-α-甘油磷酸（L-α-GP）脱氢酶被纯化了约40倍。该脱氢酶的活性虽然不受吡啶核苷酸添加的影响，但可被黄素腺嘌呤二核苷酸（Km约为10^(-7)m）刺激3至4倍，被黄素单核苷酸（Km约为10^(-4)m）刺激高达10倍。仅在两种黄素均达到饱和浓度的共同存在下才发现该酶的最大活性（刺激因子为10至15）。在两种黄素存在的情况下，反应速率对L-α-GP浓度的依赖性很复杂，但仅在黄素腺嘌呤二核苷酸存在的情况下，动力学符合米氏类型，L-α-GP的Km约为10^(-4)m。反应产物被鉴定为磷酸二羟丙酮，脱氢酶的分子量估计为80,000±10,000。吩嗪硫酸甲酯、甲萘醌和铁氰化物可作为该脱氢酶的人工受体。该酶对碘乙酸盐、对氯汞苯甲酸和N-乙基马来酰亚胺敏感。
