Kamath A V, Dasgupta D, Vaidyanathan C S
Biochem Biophys Res Commun. 1987 May 29;145(1):586-95. doi: 10.1016/0006-291x(87)91361-1.
In order to understand the molecular mechanism of non-oxidative decarboxylation of aromatic acids observed in microbial systems, 2,3 dihydroxybenzoic acid (DHBA) decarboxylase from Aspergillus niger was purified to homogeneity by affinity chromatography. The enzyme (Mr 120 kDa) had four identical subunits (28 kDa each) and was specific for DHBA. It had a pH optimum of 5.2 and Km was 0.34 mM. The decarboxylation did not require any cofactors, nor did the enzyme had any pyruvoyl group at the active site. The carboxyl group and hydroxyl group in the ortho-position were required for activity. The preliminary spectroscopic properties of the enzyme are also reported.
为了了解微生物系统中观察到的芳香酸非氧化脱羧的分子机制，通过亲和色谱法将黑曲霉的2,3 - 二羟基苯甲酸（DHBA）脱羧酶纯化至同质。该酶（Mr 120 kDa）有四个相同的亚基（每个28 kDa），对DHBA具有特异性。其最适pH为5.2，Km为0.34 mM。脱羧反应不需要任何辅因子，且该酶在活性位点也没有任何丙酮酸基团。邻位的羧基和羟基是活性所必需的。还报道了该酶的初步光谱性质。
