| Autor: |
C Carr, Roger C. Wiegand, C A Langner, J I Gordon, Robert J. Duronio, J C Minnerly, C P Carron, Adele M. Pauley |
| Rok vydání: |
1992 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 267:8591-8598 |
| ISSN: |
0021-9258 |
| DOI: |
10.1016/s0021-9258(18)42484-2 |
| Popis: |
Myristoyl-CoA:protein N-myristoyltransferase (NMT) has recently been identified as a target for antiviral and antifungal therapy. Candida albicans is a dimorphic, asexual yeast that is a major cause of systemic fungal infections in immunosuppressed humans. Metabolic labeling studies indicate that C. albicans synthesizes one principal 20-kDa N-myristoyl-protein. The single copy C. albicans NMT gene (ca-NMT1) was isolated and encodes a 451-amino acid protein that has 55% identity with Saccharomyces cerevisiae NMT. C. albicans NMT1 is able to complement the lethal phenotype of S. cerevisiae nmt1 null mutants by directing efficient acylation of the approximately 12 endogenous N-myristoylproteins produced by S. cerevisiae. C. albicans NMT was produced in Escherichia coli, a prokaryote with no endogenous NMT activity. In vitro studies of purified E. coli-derived S. cerevisiae and C. albicans NMTs revealed species-specific differences in the kinetic properties of synthetic octapeptide substrates derived from known N-myristoylproteins. Together these data indicate that C. albicans and S. cerevisiae NMTs have similar yet distinct substrate specificities which may be of therapeutic significance. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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