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Pathways to acetyl-CoA formation in Candida albicans
R Sheridan1, C Ratledge, P A Chalk
1Department of Applied Biology, University of Hull, U.K.
FEMS Microbiology Letters
|May 1, 1990
Summary
Candida albicans relies solely on carnitine acetyltransferase (CAT) for transferring acetyl units from mitochondria to the cytosol. Unlike other yeasts, it lacks ATP:citrate lyase (ACL), indicating CAT
Area of Science:
- Biochemistry
- Molecular Biology
- Mycology
Background:
- Acetyl units are crucial for various metabolic processes in Candida albicans.
- Mitochondrial export of acetyl units is essential for cytosolic functions.
- Oleaginous yeasts typically utilize ATP:citrate lyase (ACL) for acetyl-CoA production.
Purpose of the Study:
- To investigate the primary mechanism for the supply of acetyl units to the cytosol in Candida albicans.
- To determine the role of carnitine acetyltransferase (CAT) and ATP:citrate lyase (ACL) in acetyl unit translocation.
Main Methods:
- Analysis of enzyme activity and presence in both yeast and mycelial forms of Candida albicans.
- Comparative study with acetyl unit supply mechanisms in other yeast species.
Main Results:
- Carnitine acetyltransferase (CAT) activity was identified as the sole contributor to mitochondrial acetyl unit supply in Candida albicans.
- ATP:citrate lyase (ACL), a key enzyme in other yeasts, is notably absent in both yeast and mycelial forms of Candida albicans.
- No alternative pathways for acetate or acetyl group translocation were detected.
Conclusions:
- The carnitine acetyltransferase (CAT) pathway is indispensable for cytosolic acetyl unit supply in Candida albicans.
- The absence of ATP:citrate lyase (ACL) distinguishes Candida albicans' metabolic strategy from that of oleaginous yeasts.
- Understanding this unique pathway is critical for targeting Candida albicans metabolism.