Linked Life Data

15781461

Source:http://linkedlifedata.com/resource/pubmed/id/15781461

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2005-5-23
pubmed:abstractText
A soil bacterium, Burkholderia sp. WS, grows on 2-chloroacrylate as the sole carbon source. To identify the enzymes metabolizing 2-chloroacrylate, we carried out comparative two-dimensional gel electrophoresis of the proteins from 2-chloroacrylate- and lactate-grown bacterial cells. As a result, we found that a protein named CAA43 was inducibly synthesized when the cells were grown on 2-chloroacrylate. The CAA43 gene was cloned and shown to encode a protein of 333 amino acid residues (M(r) 35,788) that shared a significant sequence similarity with NADPH-dependent quinone oxidoreductase from Escherichia coli (38.2% identity). CAA43 was overproduced in E. coli and purified to homogeneity. The purified protein catalyzed the NADPH-dependent reduction of the carbon-carbon double bond of 2-chloroacrylate to produce (S)-2-chloropropionate, which is probably further metabolized to (R)-lactate by (S)-2-haloacid dehalogenase in Burkholderia sp. WS. NADH did not serve as a reductant. Despite the sequence similarity to quinone oxidoreductases, CAA43 did not act on 1,4-benzoquinone and 1,4-naphthoquinone. 2-Chloroacrylate analogs, such as acrylate and methacrylate, were also inert as the substrates. In contrast, 2-bromoacrylate served as the substrate. Thus, we named this novel enzyme 2-haloacrylate reductase. This study revealed a new pathway for the degradation of unsaturated organohalogen compounds. It is also notable that the enzyme is useful for the production of (S)-2-chloropropionate, which is used for the industrial production of aryloxyphenoxypropionic acid herbicides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20286-91
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:15781461-Acrylates, pubmed-meshheading:15781461-Amino Acid Oxidoreductases, pubmed-meshheading:15781461-Amino Acid Sequence, pubmed-meshheading:15781461-Burkholderia, pubmed-meshheading:15781461-Cloning, Molecular, pubmed-meshheading:15781461-Escherichia coli, pubmed-meshheading:15781461-Hydrogen-Ion Concentration, pubmed-meshheading:15781461-Molecular Sequence Data, pubmed-meshheading:15781461-Molecular Weight, pubmed-meshheading:15781461-NAD(P)H Dehydrogenase (Quinone), pubmed-meshheading:15781461-NADP, pubmed-meshheading:15781461-Oxidoreductases, pubmed-meshheading:15781461-Propionic Acids, pubmed-meshheading:15781461-Sequence Alignment, pubmed-meshheading:15781461-Spectrometry, Mass, Electrospray Ionization, pubmed-meshheading:15781461-Substrate Specificity, pubmed-meshheading:15781461-Temperature
pubmed:year
2005
pubmed:articleTitle
2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds.
pubmed:affiliation
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't