Jing, Ng Hong and Sulaiman, Fatin Hanani and Ab. Wahab, Roswanira and Pakinging, Rolando V., Jr. and Abdul Rashid, Noor Aini and Huyop, Fahrul (2008) Purification and properties of a non-stereospecific dehalogenase enzyme E (DehE) from Methylobacterium sp HJ1. African Journal Of Microbiology Research, 2 (7). pp. 187-191. ISSN 1996-0808
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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 K-m value for the hydrolysis of 2, 2-dichloropropionic acid was 0.25 mM. The enzyme removes chloride present on the -position, but not on the -position, of a number 2-carbon alkanoic acids.
|Uncontrolled Keywords:||haloalkanoic acid, dichloropropionate, 2, 2-dichloropropionic acid|
|Subjects:||Q Science > Q Science (General)|
|Divisions:||Biosciences and Bioengineering (Formerly known)|
|Deposited By:||Liza Porijo|
|Deposited On:||04 Jul 2011 01:30|
|Last Modified:||04 Jul 2011 01:30|
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