Manohar, R and Rao, Appu AG and Rao, Appaji N (1984) Kinetic mechanism of the interaction of D-cycloserine with serine hydroxymethyltransferase. In: Biochemistry, 23 (18). pp. 4116-4122.
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The kinetic mechanism for the interaction of D-cycloserine with serine hydroxymethyltransferase (EC220.127.116.11) from sheep liver was established by measuring changes in the activity, absorbance, and circular dichoism (CD) of the enzyme. The irreversible inhibition of the enzyme was characterized by three detectable steps: an initial rapid step followed by two successive steps with rate constants of 5.4 X s-l and 1.4 X lo4 s-l. The first step was distinguished by a rapid disappearance of the enzyme absorbance peak at 425 nm, a decrease in the enzyme activity to 25% of the uninhibited velocity, and a lowering of the CD intensity at 432 nm to about 65% of the original value. The second step of the interaction was accompanied by a complete loss of enzyme.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to American Chemical Society.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||27 Aug 2009 06:17|
|Last Modified:||19 Sep 2010 05:41|
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