Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
Volume 1680, Issue 1, Pages 60-66Publisher
ELSEVIER
DOI: 10.1016/j.bbaexp.2004.08.003
Keywords
cloning; expression; p-hydroxyphenylacetate 3-hydroxylase
Categories
Ask authors/readers for more resources
The genes encoding for the reductase and oxygenase components of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter haumannii were cloned and expressed in an E. coli system. The recombinant enzymes were purified and shown to have the same catalytic properties as the native enzyme. Sequence analysis and biochemical studies indicate that the enzyme represents a novel prototype of enzyme in the two-protein component class of aromatic hydroxylases. The C-2 component shows little similarity to other oxygenases in the same class, correlating with its uniquely broad flavin specificity. Analysis of the C-1 reductase sequence indicates that the binding sites of flavin and NADH mainly reside in the N-terminal half while the C-terminal half may be responsible for HPA-stimulation of NADH oxidation. (C) 2004 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available