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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0020364,
umls-concept:C0022818,
umls-concept:C0026584,
umls-concept:C0043395,
umls-concept:C0322859,
umls-concept:C0678941,
umls-concept:C0679058,
umls-concept:C0936012,
umls-concept:C1547699,
umls-concept:C2700640
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pubmed:issue |
5
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pubmed:dateCreated |
2003-9-16
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pubmed:abstractText |
Kynurenine 3-monooxygenase (KMO) catalyses the hydroxylation of kynurenine to 3-hydroxykynurenine. KMO has a key role in tryptophan catabolism and synthesis of ommochrome pigments in mosquitoes. The gene encoding this enzyme in the yellow fever mosquito, Aedes aegypti, is called kynurenine hydroxylase (kh) and a mutant allele that produces white eyes has been designated khw. A number of cDNA clones representative of wild-type and mutant genes were isolated. Sequence analyses of the wild-type and mutant cDNAs revealed a deletion of 162 nucleotides in the mutant gene near the 3'-end of the deduced coding region. RT-PCR analyses confirm the transcription of a truncated mRNA in the mutant strain. The in-frame deletion results in a loss of 54 amino acids, which disrupts a major alpha-helix and which probably accounts for the loss of activity of the enzyme. Recombinant Ae. aegypti KMO showed high substrate specificity for kynurenine with optimum activity at 40 degrees C and pH = 7.5. Kinetic parameters and inhibition of KMO activity by Cl- and pyridoxal-5-phosphate were determined.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10333572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10413032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10443567,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-105717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10583474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10672018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10799756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-10803381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-110313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11112172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11226705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11463462,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11514662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11805058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11880382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-11919709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-12230548,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-318458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-414739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-6501919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-6876163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-751645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-8239646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9174248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9204549,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9385648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9474782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9520437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9520438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9521324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9569641,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12974953-9575140
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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 |
0962-1075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
483-90
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12974953-Aedes,
pubmed-meshheading:12974953-Animals,
pubmed-meshheading:12974953-DNA, Complementary,
pubmed-meshheading:12974953-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12974953-Gene Deletion,
pubmed-meshheading:12974953-Gene Expression Profiling,
pubmed-meshheading:12974953-Kinetics,
pubmed-meshheading:12974953-Kynurenine 3-Monooxygenase,
pubmed-meshheading:12974953-Mixed Function Oxygenases,
pubmed-meshheading:12974953-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12974953-Sequence Alignment
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pubmed:year |
2003
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pubmed:articleTitle |
Analysis of the wild-type and mutant genes encoding the enzyme kynurenine monooxygenase of the yellow fever mosquito, Aedes aegypti.
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pubmed:affiliation |
Department of Pathobiology, University of Illinois at Urbana-Champaign, IL, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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