恶臭假单胞菌的硫辛酰胺脱氢酶与其他黄素腺嘌呤二核苷酸（FAD）连接脱氢酶的关系。

Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD-linked dehydrogenases.

作者信息

Delaney R, Burns G, Sokatch J R

出版信息

FEBS Lett. 1984 Mar 26;168(2):265-70. doi: 10.1016/0014-5793(84)80259-8.

Abstract

Pseudomonas putida produces two lipoamide dehydrogenases, LPD-glc and LPD-val. LPD-val is specifically required as the lipoamide dehydrogenase of branched-chain keto acid dehydrogenase and LPD-glc fulfills all other requirements for lipoamide dehydrogenase. Both proteins are dimers with one FAD per subunit. LPD-glc has an absorption maximum at 455 nm, but LPD-val has a maximum at 460 nm. Comparison of amino acid compositions revealed that LPD-glc was more closely related to Escherichia coli and pig heart lipoamide dehydrogenase than to LPD-val. LPD-val did not appear to be closely related to any of the proteins compared with the possible exception of mercuric reductase.

摘要

恶臭假单胞菌产生两种硫辛酰胺脱氢酶，即LPD-glc和LPD-val。LPD-val是支链酮酸脱氢酶的硫辛酰胺脱氢酶所特别需要的，而LPD-glc满足硫辛酰胺脱氢酶的所有其他需求。两种蛋白质均为二聚体，每个亚基含有一个FAD。LPD-glc在455nm处有最大吸收峰，而LPD-val在460nm处有最大吸收峰。氨基酸组成比较表明，LPD-glc与大肠杆菌和猪心硫辛酰胺脱氢酶的关系比与LPD-val的关系更密切。除了汞还原酶可能是个例外，LPD-val似乎与所比较的任何蛋白质都没有密切关系。