Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp. HJ1
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The bacterial isolate HJ1, which was identified as a Methylobacterium sp., grew on 2, 2-dichloropropionic acid as the sole carbon source and produced a 2-haloalkanoic acid hydrolytic dehalogenase. This non-stereospecific dehalogenase E (DehE) catalysed the hydrolytic dechlorination of 2, 2-dichloropropionic acid and D, L-2-chloropropionic acid to produce pyruvate and lactate, respectively. The enzyme was purified to homogeneity and characterized. The molecular weight was 36 kDa by SDS-polyacrylamide gel electrophoresis and 72 kDa by gel filtration, suggesting that the enzyme is a protein dimer. The purified enzyme was only inhibited by HgSO4 and was non-stereospecific to haloalkanoic acids. The Km value for the hydrolysis of 2, 2-dichloropropionic acid was 0.25 mM. The enzyme removes chloride present on the α-position, but not on the β-position, of a number 2-carbon alkanoic acids.
Jing, N. H., Sulaiman, F. H., Wahab, R. A., Pakingking, R. V., Jr., Rashid, N. A. A., & Huyop, F. (2008). Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp. HJ1.
African Journal of Microbiology Research, 2(7), 187-191. http://hdl.handle.net/10862/2081
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