Mahadevan U, Padmanaban G
Department of Biochemistry, Indian Institute of Science, Bangalore, India.
Biochem Biophys Res Commun. 1998 Mar 27;244(3):893-7. doi: 10.1006/bbrc.1998.8354.
A gene from Mycobacterium tuberculosis coding for acyl-CoA dehydrogenase was cloned, overexpressed and characterized on the basis of enzyme activity with various chain length substrates. The results show that the protein is a medium chain acyl-CoA dehydrogenase (MCADH). The mycobacterium protein expressed appears to be unique, since by comparison, the active site glutamic acid of the protein does not lie in the same position as other well characterized MCADH, but in a position present in long chain and isovaleryl acyl-CoA dehydrogenases (LCADH and IVDH).
克隆了结核分枝杆菌中一个编码酰基辅酶A脱氢酶的基因,对其进行了过表达,并根据其对各种链长底物的酶活性进行了表征。结果表明该蛋白是一种中链酰基辅酶A脱氢酶(MCADH)。所表达的分枝杆菌蛋白似乎是独特的,因为相比之下,该蛋白的活性位点谷氨酸并不位于与其他特征明确的MCADH相同的位置,而是位于长链和异戊酰基辅酶A脱氢酶(LCADH和IVDH)中的一个位置。