Abstract 2491 Functional Characterization of ATP-Citrate Lyase Mutants in Yarrowia lipolytica

ATP citrate lyase catalyzes the ATP-dependent conversion of citrate to acetyl-CoA, an indispensable intermediate in lipid biosynthesis. The Yarrowia lipolytica ACL enzyme is a heterodimeric protein composed of the catalytic subunit Acl1 and the regulatory subunit Acl2. Mutants deficient in ACL exhibit diminished lipid levels and a global transcriptional reprogramming. In this work, we investigated the phenotypic effects of the ablation of each ACL subunit on growth and carbon source utilization.

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Publication Details

Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.109435
Citations
1
Primary Topic
Microbial Metabolic Engineering and Bioproduction
Type
article
Field-Weighted Citation Impact
0.81
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article

Abstract 2491 Functional Characterization of ATP-Citrate Lyase Mutants in Yarrowia lipolytica

Stylianos Fakas, Ayodeji Odunsi
1 citations
Journal of Biological Chemistry
Microbial Metabolic Engineering and Bioproduction
0.81
article

Abstract 2491 Functional Characterization of ATP-Citrate Lyase Mutants in Yarrowia lipolytica

Stylianos Fakas, Ayodeji Odunsi
article en
1 citations

Abstract

ATP citrate lyase catalyzes the ATP-dependent conversion of citrate to acetyl-CoA, an indispensable intermediate in lipid biosynthesis. The Yarrowia lipolytica ACL enzyme is a heterodimeric protein composed of the catalytic subunit Acl1 and the regulatory subunit Acl2. Mutants deficient in ACL exhibit diminished lipid levels and a global transcriptional reprogramming. In this work, we investigated the phenotypic effects of the ablation of each ACL subunit on growth and carbon source utilization.

Journal of Biological ChemistryVol. 301(5)
Florida Agricultural and Mechanical University (US)
Zero hunger
Openalex Percentile: Top 27%
Microbial Metabolic Engineering and Bioproduction
0.81
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