Rajasekharan, Sumathi and Rajasekharan, Ram and Vaidyanathan, CS (1990) Substrate-mediated purification and characterization of a 3-hydroxybenzoic acid-6-hydroxylase from Micrococcus. In: Archives of Biochemistry and Biophysics, 278 (1). pp. 21-25.
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3-Hydroxybenzoic acid-6-hydroxylase from Micrococcus sp. was purified to homogeneity in a single step using the substrate-mediated interaction of the enzyme with blue-Sepharose. The enzyme was bound to the affinity matrix in the presence of 3-hydroxybenzoic acid and was eluted in its absence. The molecular weight of the purified enzyme is 70,000 with no subunit structure. The flavoenzyme required the exogenous addition of FAD for its complete activity and had a strict preference for NADH over NADPH. The activity of the enzyme was drastically inhibited by Cu2+ and Hg2+ and the inhibition was reversed by thiol reagents.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||11 Jan 2011 08:44|
|Last Modified:||11 Jan 2011 08:44|
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