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Biochemical characterization of recombinant dihydroorotate dehydrogenase from the opportunistic pathogenic yeast Candida albicansZameitat, Elke ...Candida albicans is the most prevalent yeast pathogen in humans, and recently it has become increasingly resistant to the current antifungal agents. In thisstudy we investigated C. albicans ... dihydroorotate dehydrogenase (DHODH, EC 1.3.99.11), which catalyzes the fourth step of de novo pyrimidine synthesis, as a new target for controlling infection. We propose that the enzyme is a member of the DHODH family 2, which comprises mitochondrially bound enzymes, with quinone as the direct electron acceptor and oxygen as the final electron acceptor. Full-length DHODH and N-terminally truncated DHODH, which lacks the targeting sequence and the transmembrane domain, were subcloned from C. albicans, recombinantly expressed in Escherichia coli, purified, and characterized for their kinetics and substrate specificity. An inhibitor screening with 28 selected compounds was performed. Only the dianisidine derivative, redoxal, and the biphenyl quinoline-carboxylic acid derivative, brequinar sodium, which are known to be potent inhibitors of mammalian DHODH, markedly reduced C. albicans DHODH activity. This study provides a background for the development of antipyrimidines with high efficacy for decreasing in situ pyrimidine nucleotide pools in C. albicans.Vir: FEBS journal. - ISSN 1742-464X (Letn. 273, št. 14, 2006, str. 3183-3191)Vrsta gradiva - članek, sestavni delLeto - 2006Jezik - angleškiCOBISS.SI-ID - 25358553
Avtor
Zameitat, Elke |
Gojković, Zoran |
Knecht, Wolfgang |
Piškur, Jure, 1960-2014 |
Löffler, Monika
Teme
Amino Acid Sequence |
Aminobiphenyl Compounds |
Metabolism |
Pharmacology |
Biphenyl Compounds |
Metabolism |
Pharmacology |
Candida Albicans |
Enzymology |
Pathogenicity |
Conserved Sequence |
Enzyme Inhibitors |
Metabolism |
Pharmacology |
Escherichia Coli |
Genetics |
Hydrogen-Ion Concentration |
Kinetics |
Molecular Sequence Data |
Molecular Structure |
Mutation |
Protein Structure, Tertiary |
Recombinant Fusion Proteins |
Chemistry |
Isolation & Purification |
Metabolism |
Sequence Homology, Amino Acid |
Substrate Specificity |
Substrat, specifičnost |
Molekulsko zaporedje, podatki |
Rekombinantne, fuzijske beljakovine |
Escherichia coli |
Shranjeno zaporedje |
Beljakovinska struktura terciarna |
Zaporedna homolognost aminokislin |
Kinetika |
Aminobifenilne spojine |
Encimski inhibitorji |
Aminokislinsko zaporedje |
Bifenilne spojine |
Candida albicans |
pH |
Molekularna struktura |
Mutacija
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Zameitat, Elke | ![]() |
Gojković, Zoran | ![]() |
Knecht, Wolfgang | ![]() |
Piškur, Jure, 1960-2014 | 31275 |
Löffler, Monika | ![]() |
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