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The masked cysteine residues in methylmalonyl-CoA mutase from Propionibacterium shermanii are essential for catalytic activity

Roy, Ipsita (1996) The masked cysteine residues in methylmalonyl-CoA mutase from Propionibacterium shermanii are essential for catalytic activity. FEBS Letters , 394 (2). pp. 126-128. ISSN 0014-5793

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Official URL: http://dx.doi.org/10.1016/0014-5793(96)00897-6

Abstract

Two masked cysteine residues have been reported in methylmalonyl-CoA mutase from Propionibacterium shermanii, Cys-535 in the α-subunit and Cys-517 in the β-unit, which are revealed only after reduction of the denatured enzyme with dithiothreitol. It has been postulated that these residues are involved in disulphide linkages to unknown thiols of low Mr. These two masked cysteine residues have been changed to an alanine, individually. Both the mutants, C535αA and C517βA, were inactive. This shows that both these residues are essential for catalytic activity.

Item Type:Article
Research Community:University of Westminster > Life Sciences, School of
ID Code:7126
Deposited On:07 Jan 2010 11:01
Last Modified:07 Jan 2010 11:01

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