Kimura K
J Biochem. 1975 Feb;77(2):405-13. doi: 10.1093/oxfordjournals.jbchem.a130739.
A dihydrodipicolinate reductase containing flavin was purified from sporulating Bacillus subtilis PCI 219. The purified enzyme appeared homogeneous by dise gel electrophoresis. Its molecular weight was estimated as 74,000 by gel filtration on Sephadex G-200, and as 18,500 by electrophoresis on sodium dodecylsulfate polyacrylamid gel. These results suggest that the enzyme is composed of four subunits. The prosthetic group was identified as FMN, and one mole of the enzyme contained two moles of FMN. Both NADPH and NADH acted as coenzyme, though NADH was less effective. The enzyme also exhibited diaphorase activity. The pH optimum was 6.1. The enzyme was inhibited by dipicolinate but not by lysine or alpha, epsilon-diaminopimelate.
从枯草芽孢杆菌PCI 219的芽孢形成细胞中纯化出一种含黄素的二氢二吡啶甲酸还原酶。经圆盘凝胶电泳分析，纯化后的酶呈现均一性。通过Sephadex G - 200凝胶过滤法估算其分子量为74,000，通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳法估算为18,500。这些结果表明该酶由四个亚基组成。其辅基被鉴定为FMN，每摩尔酶含有两摩尔FMN。NADPH和NADH均可作为辅酶，不过NADH的效果稍差。该酶还具有黄递酶活性。最适pH为6.1。该酶受二吡啶甲酸盐抑制，但不受赖氨酸或α,ε - 二氨基庚二酸抑制。
