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rdf:type |
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lifeskim:mentions |
umls-concept:C0001963,
umls-concept:C0080194,
umls-concept:C0205463,
umls-concept:C0599833,
umls-concept:C0871261,
umls-concept:C1295863,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C1880022,
umls-concept:C1998793,
umls-concept:C2911692
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pubmed:issue |
2
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pubmed:dateCreated |
2003-10-13
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pubmed:abstractText |
A novel catalase-peroxidase (CP) from methanol-grown cells of Mycobacterium sp. strain JC1 was purified. The CP exhibited properties of both typical mycobacterial CPs (i.e. strict pH optimum, labile to heat treatment, capable of oxidizing NADH, and resistant to inhibition by 3-amino-1,2,4-triazole) and true catalases (i.e. stable against ethanol-chloroform treatment). The enzyme oxidized methanol and shared common antigenic groups with other mycobacteria. Isoniazid had almost no effect on the growth and expression of CP but inhibited the enzyme activity to some extent. Sodium nitroprusside arrested the growth but strongly stimulated the expression of CP with a concomitant increase in activity after the mid-exponential growth phase.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Amitrole,
http://linkedlifedata.com/resource/pubmed/chemical/Antitubercular Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chloroform,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Isoniazid,
http://linkedlifedata.com/resource/pubmed/chemical/Methanol,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroprusside,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/catalase-peroxidase, bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0378-1097
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
226
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
397-403
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:14553939-Amitrole,
pubmed-meshheading:14553939-Antitubercular Agents,
pubmed-meshheading:14553939-Bacterial Proteins,
pubmed-meshheading:14553939-Chloroform,
pubmed-meshheading:14553939-Dimerization,
pubmed-meshheading:14553939-Enzyme Inhibitors,
pubmed-meshheading:14553939-Enzyme Stability,
pubmed-meshheading:14553939-Gene Expression,
pubmed-meshheading:14553939-Hot Temperature,
pubmed-meshheading:14553939-Hydrogen-Ion Concentration,
pubmed-meshheading:14553939-Isoelectric Point,
pubmed-meshheading:14553939-Isoniazid,
pubmed-meshheading:14553939-Methanol,
pubmed-meshheading:14553939-Molecular Weight,
pubmed-meshheading:14553939-Mycobacterium,
pubmed-meshheading:14553939-NAD,
pubmed-meshheading:14553939-Nitroprusside,
pubmed-meshheading:14553939-Oxidation-Reduction,
pubmed-meshheading:14553939-Peroxidases,
pubmed-meshheading:14553939-Protein Subunits,
pubmed-meshheading:14553939-Substrate Specificity
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pubmed:year |
2003
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pubmed:articleTitle |
Purification, characterization, and physiological response of a catalase-peroxidase in Mycobacterium sp. strain JC1 DSM 3803 grown on methanol.
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pubmed:affiliation |
Laboratory of Biochemistry, College of Medicine, Konkuk University, Chungju 380-701, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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