Shimao M, Ninomiya K, Kuno O, Kato N, Sakazawa C
Appl Environ Microbiol. 1986 Feb;51(2):268-75. doi: 10.1128/aem.51.2.268-275.1986.
A novel enzyme, pyrroloquinoline quinone (PQQ)-dependent polyvinyl alcohol (PVA) dehydrogenase, was found in and partially purified from the membrane fraction of a PVA-degrading symbiont, Pseudomonas sp. strain VM15C. The enzyme required PQQ for PVA dehydrogenation with phenazine methosulfate, phenazine ethosulfate, and 2,6-dichlorophenolindophenol as electron acceptors and did not show PVA oxidase activity leading to H2O2 formation. The enzyme was active toward low-molecular-weight secondary alcohols rather than primary alcohols. A membrane-bound PVA oxidase was also present in cells of VM15C. Although the purified oxidase showed a substrate specificity similar to that of PQQ-dependent PVA dehydrogenase and about threefold-higher PVA-dehydrogenating activity with phenazine methosulfate or phenazine ethosulfate than PVA oxidase activity with H2O2 formation, it was shown that the enzyme does not contain PQQ as the coenzyme, and PQQ did not affect its activity. Incubation of the membrane fraction of cells with PVA caused a reduction in the cytochrome(s) of the fraction.
在一株降解聚乙烯醇（PVA）的共生菌——假单胞菌属VM15C菌株的膜组分中发现了一种新型酶，即吡咯喹啉醌（PQQ）依赖性聚乙烯醇脱氢酶，并对其进行了部分纯化。该酶以吩嗪硫酸甲酯、吩嗪硫酸乙酯和2,6-二氯酚靛酚作为电子受体进行PVA脱氢反应时需要PQQ，且不表现出导致过氧化氢形成的PVA氧化酶活性。该酶对低分子量仲醇有活性，而对伯醇无活性。VM15C细胞中还存在一种膜结合的PVA氧化酶。尽管纯化的氧化酶表现出与PQQ依赖性PVA脱氢酶相似的底物特异性，且以吩嗪硫酸甲酯或吩嗪硫酸乙酯作为电子受体时的PVA脱氢活性比导致过氧化氢形成的PVA氧化酶活性高约三倍，但结果表明该酶不含PQQ作为辅酶，且PQQ不影响其活性。用PVA孵育细胞的膜组分导致该组分中细胞色素减少。
