Sumathi, S and Dasgupta, D and Vaidyanathan, CS (1998) Chemical modification of 3-HBA-6-hydroxylase by phenylglyoxal: Kinetic acid physicochemical studies on the modified enzyme. In: Indian Journal of Biochemistry and Biophysics, 35 (5). pp. 266-272.Full text not available from this repository. (Request a copy)
The inactivation of 3-HBA-6-hydroxylase isolated from Micrococcus species by phenylglyoxal and protection offered by 3-HBA against inactivation indicate the presence of arginine residue at or near the substrate binding site. The loss of enzyme activity was time and concentration dependent and displayed pseudo-first order kinetics. a 'n' value of 0.9 was obtained thus suggesting the modification of a single arginine residue per active site which led to the loss of enzyme activity. The enzyme activity could be restored by extensive dialysis at neutral pH. Quenching of the intrinsic fluorescence and reduction in the ellipticity value at 280 nm in the near-UV CD spectrum of the enzyme was noticed after its treatment with phenylglyoxal. These observations probably imply distinct perturbations in the environment of adjacent aromatic amino acid residues such as tryptophan as a consequence of arginine modification.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to National Institute Science Communication and Information Resources.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||28 May 2009 09:21|
|Last Modified:||28 May 2009 09:21|
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