Linked Life Data

7103659

Source:http://linkedlifedata.com/resource/pubmed/id/7103659

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-9-17
pubmed:abstractText
The occurrence of a new bacterial dehalogenase acting on both the optical isomers of 2-halogenated alkanoic acids was demonstrated. When the haloalkanoic acid-utilizing bacteria were screened in a medium containing DL-2-chloropropionate as a sole carbon source, two types of bacteria were isolated: (1) a few strains utilizing both D- and L-isomers of 2-chloropropionate and (2) strains utilizing only the L-isomer. A dehalogenating enzyme was obtained from the cells of Pseudomonas sp. which is able to utilize both isomers. The crude enzyme catalyzed the dehalogenation of D- and L-2-chloropropionates to yield L- and D-isomers of lactate, respectively. The enzyme showed the same pH optimum and heat inactivation rate for the D- and L-isomers. Apparent Km values for D- and L-2-chloropropionates were 4.5 and 1.0mM, respectively. The enzyme acted specifically on 2-haloalkanoic acids. Activity staining of disc-gels electrophoresed with the crude enzyme preparation showed that the dehalogenation of D- and L-2-chloropropionates, monochloroacetate, dichloroacetate, 2,2-dichloropropionate, and DL-2-chlorobutyrate is due to a single protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0302-8933
pubmed:author
pubmed:issnType
Print
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
179-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Bacterial assimilation of D- and L-2-chloropropionates and occurrence of a new dehalogenase.
pubmed:publicationType
Journal Article, Comparative Study