| pubmed-article:16681373 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16681373 | lifeskim:mentions | umls-concept:C0022262 | lld:lifeskim |
| pubmed-article:16681373 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:16681373 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:16681373 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16681373 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:16681373 | pubmed:dateCreated | 2006-5-9 | lld:pubmed |
| pubmed-article:16681373 | pubmed:abstractText | dl-2-Haloacid dehalogenase from Pseudomonas sp. 113 is a unique enzyme because it acts on the chiral carbons of both enantiomers, although its amino acid sequence is similar only to that of d-2-haloacid dehalogenase from Pseudomonas putida AJ1 that specifically acts on (R)-(+)-2-haloalkanoic acids. Furthermore, the catalyzed dehalogenation proceeds without formation of an ester intermediate; instead, a water molecule directly attacks the alpha-carbon of the 2-haloalkanoic acid. We have studied solvent deuterium and chlorine kinetic isotope effects for both stereoisomeric reactants. We have found that chlorine kinetic isotope effects are different: 1.0105 +/- 0.0001 for (S)-(-)-2-chloropropionate and 1.0082 +/- 0.0005 for the (R)-(+)-isomer. Together with solvent deuterium isotope effects on V(max)/K(M), 0.78 +/- 0.09 for (S)-(-)-2-chloropropionate and 0.90 +/- 0.13 for the (R)-(+)-isomer, these values indicate that in the case of the (R)-(+)-reactant another step preceding the dehalogenation is partly rate-limiting. Under the V(max) conditions, the corresponding solvent deuterium isotope effects are 1.48 +/- 0.10 and 0.87 +/- 0.27, respectively. These results indicate that the overall reaction rates are controlled by different steps in the catalysis of (S)-(-)- and (R)-(+)-reactants. | lld:pubmed |
| pubmed-article:16681373 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16681373 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681373 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16681373 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681373 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16681373 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16681373 | pubmed:month | May | lld:pubmed |
| pubmed-article:16681373 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:Rudzi?skiJuli... | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:PanethPiotrP | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:EsakiNobuyosh... | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:KuriharaTatsu... | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:Kami?skiRafa... | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:Kwiecie?Renat... | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:PapajakEwaE | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:Sici?skaDaria... | lld:pubmed |
| pubmed-article:16681373 | pubmed:author | pubmed-author:Szatkowski?uk... | lld:pubmed |
| pubmed-article:16681373 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16681373 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:16681373 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:16681373 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16681373 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16681373 | pubmed:pagination | 6012-7 | lld:pubmed |
| pubmed-article:16681373 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16681373 | pubmed:meshHeading | pubmed-meshheading:16681373... | lld:pubmed |
| pubmed-article:16681373 | pubmed:meshHeading | pubmed-meshheading:16681373... | lld:pubmed |
| pubmed-article:16681373 | pubmed:meshHeading | pubmed-meshheading:16681373... | lld:pubmed |
| pubmed-article:16681373 | pubmed:meshHeading | pubmed-meshheading:16681373... | lld:pubmed |
| pubmed-article:16681373 | pubmed:meshHeading | pubmed-meshheading:16681373... | lld:pubmed |
| pubmed-article:16681373 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16681373 | pubmed:articleTitle | Mechanism of the reaction catalyzed by DL-2-haloacid dehalogenase as determined from kinetic isotope effects. | lld:pubmed |
| pubmed-article:16681373 | pubmed:affiliation | Institute of Radiation Chemistry, Department of Chemistry, Technical University of Lodz, Zeromskiego 116, 90-924 Lodz, Poland. | lld:pubmed |
| pubmed-article:16681373 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16681373 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
