Takahashi S, Abbe K, Yamada T
J Bacteriol. 1982 Mar;149(3):1034-40. doi: 10.1128/jb.149.3.1034-1040.1982.
Pyruvate formate-lyase (EC 2.3.1.54) from Streptococcus mutans strain JC2 was purified in an anaerobic glove box, giving a single band on disk and sodium dodecyl sulfate electrophoresis. This enzyme was immediately inactivated by exposure to the air. Enzyme activity was unstable even when stored anaerobically, but the activity was restored by preincubating the inactivated crude enzyme with S-adenosyl-L-methionine, oxamate, and reduced for ferredoxin or methylviologen. On the other hand, the purified enzyme was not reactivated. Either D-glyceraldehyde 3-phosphate or dihydroxyacetone phosphate strongly inhibited this enzyme. The inhibitory effects of these compounds were largely influenced by enzyme concentration. The inhibition of these triose phosphates in cooperation with the reactivating effect of ferredoxin and the fluctuations of both the enzyme and the triose phosphate levels may efficiently regulate the pyruvate formate-lyase activity in S. mutans in vivo.
来自变形链球菌JC2菌株的丙酮酸甲酸裂解酶（EC 2.3.1.54）在厌氧手套箱中进行纯化，在圆盘电泳和十二烷基硫酸钠电泳上呈现单一谱带。该酶暴露于空气中会立即失活。即使在厌氧条件下储存，酶活性也不稳定，但通过将失活的粗酶与S-腺苷-L-甲硫氨酸、草氨酸以及还原型铁氧还蛋白或甲基紫精预孵育，活性可恢复。另一方面，纯化后的酶无法再激活。3-磷酸-D-甘油醛或磷酸二羟丙酮强烈抑制该酶。这些化合物的抑制作用在很大程度上受酶浓度影响。这些磷酸丙糖的抑制作用与铁氧还蛋白的再激活作用以及酶和磷酸丙糖水平的波动共同作用，可能在体内有效调节变形链球菌中丙酮酸甲酸裂解酶的活性。
