Source:http://linkedlifedata.com/resource/pubmed/id/12619671
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-3-6
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pubmed:abstractText |
2-Hydroxy-6-oxo-6-(2'-aminophenyl)-hexa-2,4dienoic acid [6-(2'-aminophenyl)-HODA] hydrolase, involved in carbazole degradation by Pseudomonas resinovorans strain CA10, was purified to near homogeneity from an overexpressing Escherichia coli strain. The enzyme was dimeric, and its optimum pH was 7.0-7.5. Phylogenetic analysis showed the close relationship of this enzyme to other hydrolases involved in the degradation of monocyclic aromatic compounds, and this enzyme was specific for 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (6-phenyl-HODA), having little activity toward 2-hydroxy-6-oxohepta-2,4-dienoic acid and 2-hydroxymuconic semialdehyde. The enzyme had a Km of 2.51 microM and k(cat) of 2.14 (s(-1)) for 6-phenyl-HODA (50 mM sodium phosphate, pH 7.5, 25 degrees C). The effect of the presence of an amino group or hydroxyl group at the 2'-position of phenyl moiety of 6-phenyl-HODA on the enzyme activity was found to be small; the activity decreased only in the order of 6-(2'-aminophenyl)-HODA (2.44 U/mg) > 6-phenyl-HODA (1.99 U / mg) > 2-hydroxy-6-oxo-6-(2'-hydroxyphenyl)-hexa-2,4-dienoic acid (1.05 U/mg). The effects of 2'-substitution on the activity were in accordance with the predicted reactivity based on the calculated lowest unoccupied molecular orbital energy for these substrates.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0916-8451
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pubmed:author |
pubmed-author:HabeHiroshiH,
pubmed-author:IwataKenichiK,
pubmed-author:MoriiKenichiK,
pubmed-author:NakamuraShugoS,
pubmed-author:NamJeong-WonJW,
pubmed-author:NojiriHideakiH,
pubmed-author:OmoriToshioT,
pubmed-author:ShimizuKentaroK,
pubmed-author:TairaHirokoH,
pubmed-author:TakadaYoshikiY,
pubmed-author:YamaneHisakazuH
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pubmed:issnType |
Print
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36-45
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12619671-Biotransformation,
pubmed-meshheading:12619671-Carbazoles,
pubmed-meshheading:12619671-Culture Media,
pubmed-meshheading:12619671-DNA, Bacterial,
pubmed-meshheading:12619671-Escherichia coli,
pubmed-meshheading:12619671-Hydrogen-Ion Concentration,
pubmed-meshheading:12619671-Hydrolases,
pubmed-meshheading:12619671-Kinetics,
pubmed-meshheading:12619671-Phylogeny,
pubmed-meshheading:12619671-Plasmids,
pubmed-meshheading:12619671-Pseudomonas,
pubmed-meshheading:12619671-Structure-Activity Relationship,
pubmed-meshheading:12619671-Temperature
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pubmed:year |
2003
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pubmed:articleTitle |
Purification and characterization of meta-cleavage compound hydrolase from a carbazole degrader Pseudomonas resinovorans strain CA10.
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pubmed:affiliation |
Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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