NDLI: Purification and characterization of D-2-haloacid dehalogenase from Pseudomonas putida strain AJ 1 / 23

Content Provider	Semantic Scholar
Author	Smith, J. M. Harrison, Karen John
Copyright Year	2008
Abstract	A D-2-haloacid dehalogenase was isolated and purified to homogeneity from Pseudomonas p u t i h strain AJ1/23. The enzyme catalysed the stereospecific dehalogenation of the D-isomer of 2-chloropropionate. Using a new ionchromatograph assay, the enzyme was found to catalyse the dehalogenation of short-chain 2-halocarboxylic acids. Maximum enzyme activity occurred at pH 9.5 and 50 "C and the enzyme was insensitive to most S H reagents. The enzyme has an M, of about 135000 and appears to be composed of four subunits of identical Mr.
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Alternate Webpage(s)	http://www.microbiologyresearch.org/docserver/fulltext/micro/136/5/mic-136-5-881.pdf?accname=guest&checksum=7C42A112D848A4AC694921346F0F726B&expires=1544728628&id=id
Alternate Webpage(s)	http://www.microbiologyresearch.org/docserver/fulltext/micro/136/5/mic-136-5-881.pdf?accname=guest&checksum=F5E7EA0E153177C087C6B4A5514A8973&expires=1541035900&id=id
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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