Haribabu, B and Rao, NA and Vaidyanathan, CS (1985) An essential arginine residue at the substrate binding site of 4-hydroxyisophthalate hydroxylase. In: Biochemistry International, 11 (6). pp. 773-780.Full text not available from this repository. (Request a copy)
4-Hydroxyisophthalate hydroxylase was inactivated by treatment with phenylglyoxal by a process obeying pseudo-first order kinetics indicating the presence of an essential arginine located presumably in the active site. Addition of saturating amounts of 4-hydroxyisophthalate during the treatment resulted in complete protection of the enzyme from the inactivation, but addition of NADPH was totally ineffective. Analysis of the effect of various substrate analogs on the protection of the enzyme showed that carboxyl and hydroxyl groups at para positions on the aromatic ring are essential for substrate binding to the active site. It was also observed that analogs which protect the enzyme against phenylglyoxal inactivation are themselves effective inhibitors of the enzyme activity.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Academic press aust.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||27 Jan 2010 06:30|
|Last Modified:||27 Jan 2010 06:30|
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