荧光假单胞菌PHK中的邻苯二甲酸酯代谢：4,5-二羟基邻苯二甲酸脱羧酶的纯化及特性
Phthalate metabolism in Pseudomonas fluorescens PHK: purification and properties of 4,5-dihydroxyphthalate decarboxylase.
作者信息
Pujar B G, Ribbons D W
出版信息
Appl Environ Microbiol. 1985 Feb;49(2):374-6. doi: 10.1128/aem.49.2.374-376.1985.
Abstract
Pseudomonas fluorescens PHK uses 4,5-dihydroxyphthalate as the sole carbon source for o-phthalate catabolism. This intermediate is the substrate for a decarboxylase of the pathway yielding protocatechuate. The decarboxylase was purified to homogeneity by an affinity chromatography procedure in which the reaction product, protocatechuate, was used as a ligand. We describe some properties of the enzyme, including its apparent molecular weight of 420,000 as determined by gel filtration and of 66,000 after sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis, consistent with a hexameric functional protein. The apparent Km for the substrate 4,5-dihydroxyphthalate was 10.4 microM. The characteristics of this enzyme are compared with those described for the isofunctional enzyme from P. testosteroni.
摘要
荧光假单胞菌PHK利用4,5-二羟基邻苯二甲酸作为邻苯二甲酸分解代谢的唯一碳源。这种中间产物是该途径中一种脱羧酶的底物，可生成原儿茶酸。通过亲和层析法将该脱羧酶纯化至同质，其中反应产物原儿茶酸用作配体。我们描述了该酶的一些特性，包括通过凝胶过滤测定的表观分子量为420,000，在十二烷基硫酸钠-聚丙烯酰胺圆盘凝胶电泳后为66,000，这与六聚体功能蛋白一致。底物4,5-二羟基邻苯二甲酸的表观Km为10.4 microM。将该酶的特性与睾丸酮假单胞菌的同功能酶的特性进行了比较。
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