Relationship of lipoamide dehydrogenases from Pseudomonas putida to other FAD‐linked dehydrogenases

FEBS Letters

Burns, Gayle¹  Delaney, Robert²  Sokatch, John R.¹ 

[1] Department of Microbiology and Immunology, The University of Oklahoma Health Sciences Center, PO Box 26901, Oklahoma City, OK 73190, USA;Department of Biochemistry and Molecular Biology, The University of Oklahoma Health Sciences Center, PO Box 26901, Oklahoma City, OK 73190, USA

关键词: Lipoamide dehydrogenase;    Branched-chain keto acid dehydrogenase;    Pseudomonas putida;   

DOI  :  10.1016/0014-5793(84)80259-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown