Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand

Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand
复制标题

DOI:
10.1271/bbb.69.1120
复制
发表时间:
2005-06-01
影响因子:
1.6
通讯作者:
Matsushita, K
Matsushita, K
中科院分区:
工程技术4区
文献类型:
--
作者:
Toyama, H;Soemphol, W;Matsushita, K

文献摘要

被引文献

相似文献

已报道的膜结合D-山梨醇脱氢酶(SLDH)有两种类型:PQQ-SLDH,含有吡咯喹啉醌(PQQ),和FAD-SLDH,含有FAD和血红素c作为辅基。FAD-SLDH是从耐高温的Frateurii葡萄糖酸杆菌的PQQ-SLDH突变株中纯化并表征的,其分子量为61.5kDa、52 kDa和22 kDa。该酶的性质与嗜中温G.第3254章.这种酶被证明是由D-山梨醇诱导,但不是PQQ SLDH。D-山梨醇的FAD-SLDH氧化产物经鉴定为L-山梨糖。克隆的FAD-SLDH基因具有3个开放阅读框架(sldSLC),分别对应于FAD-SLDH的小亚基、大亚基和细胞色素c亚基。推导的氨基酸序列与G.氧化物IFO 3254:SIdC具有三个血红素C结合基序,与其它膜结合型辅酶A酶的细胞色素C亚基结合。
There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluconobacter frateurii, having molecular mass of 61.5 kDa, 52kDa, and 22kDa. The enzyme properties were quite similar to those of the enzyme from mesophilic G. oxydans IFO 3254. This enzyme was shown to be inducible by D-sorbitol, but not PQQ SLDH. The oxidation product of FAD-SLDH from D-sorbitol was identified as L-sorbose. The cloned gene of FAD-SLDH had three open reading frames (sldSLC) corresponding to the small, the large, and cytochrome c subunits of FAD-SLDH respectively. The deduced amino acid sequences showed high identity to those from G. oxydans IFO 3254: SIdL showed to other FAD-enzymes, and SldC having three heme c binding motives to cytochrome c subunits of other membrane-bound dehydrogenases.