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rdf:type |
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lifeskim:mentions |
umls-concept:C0004611,
umls-concept:C0009015,
umls-concept:C0017262,
umls-concept:C0017337,
umls-concept:C0080194,
umls-concept:C0185117,
umls-concept:C0679058,
umls-concept:C0772162,
umls-concept:C1295863,
umls-concept:C1547699,
umls-concept:C1880022,
umls-concept:C2700640,
umls-concept:C2911684
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pubmed:issue |
10
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pubmed:dateCreated |
2000-10-17
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pubmed:databankReference |
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pubmed:abstractText |
A 81-kDa protein from Mycobacterium sp. strain PYR-1 was expressed in response to exposure of the strain to the polycyclic aromatic hydrocarbon pyrene and recovered by two-dimensional gel electrophoresis. The N-terminal sequence of the protein indicated that it was similar to catalase-peroxidase. An oligonucleotide probe designed from this sequence was used to screen a genomic library of Mycobacterium sp. strain PYR-1, and a positive clone, containing a part of the gene encoding the 81-kDa protein, was isolated. A gene-walking technique was used to sequence the entire gene, which was identified as katG for catalase-peroxidase. The deduced KatG protein sequence showed significant homology to KatGII of Mycobacterium fortuitum and clustered with catalase-peroxidase proteins from other Mycobacterium species in a phylogenetic tree. The katG gene was expressed in Escherichia coli to produce a protein with catalase-peroxidase activity. Since the induction of this catalase-peroxidase occurred in pyrene-induced cultures and the exposure of these cultures to hydrogen peroxide reduced pyrene metabolism, our data suggest that this enzyme plays a role in polycyclic aromatic hydrocarbon metabolism by strain PYR-1.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-10217759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-1501713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-15091809,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-1785924,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-2782874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-3189820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-3202633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-3202634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-7604044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-7811065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-7867972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-8328808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-8621411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-9105615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-9254694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-9371430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11010873-942051
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0099-2240
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4300-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:11010873-Bacterial Proteins,
pubmed-meshheading:11010873-Base Sequence,
pubmed-meshheading:11010873-Cloning, Molecular,
pubmed-meshheading:11010873-Escherichia coli,
pubmed-meshheading:11010873-Genetic Vectors,
pubmed-meshheading:11010873-Hydrogen Peroxide,
pubmed-meshheading:11010873-Kinetics,
pubmed-meshheading:11010873-Molecular Sequence Data,
pubmed-meshheading:11010873-Mycobacterium,
pubmed-meshheading:11010873-Peroxidases,
pubmed-meshheading:11010873-Phylogeny,
pubmed-meshheading:11010873-Plasmids,
pubmed-meshheading:11010873-Polycyclic Hydrocarbons, Aromatic,
pubmed-meshheading:11010873-Pyrenes,
pubmed-meshheading:11010873-Recombinant Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
Cloning, expression, and characterization of the katG gene, encoding catalase-peroxidase, from the polycyclic aromatic hydrocarbon-degrading bacterium Mycobacterium sp. strain PYR-1.
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pubmed:affiliation |
Microbiology Division, National Center for Toxicological Research, Food and Drug Administration, Jefferson, Arkansas 72079, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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