Off-Loading Mechanism of Products in Polyunsaturated Fatty Acid Synthases
- Resource Type
- Authors
- Chitose Maruyama; Tohru Dairi; Yoshimitsu Hamano; Yasuharu Satoh; Yasushi Ogasawara; Shohei Hayashi
- Source
- ACS Chemical Biology. 15:651-656
- Subject
- 0301 basic medicine
Fatty Acid Synthases
Docosahexaenoic Acids
01 natural sciences
Biochemistry
Catalysis
Substrate Specificity
Structure-Activity Relationship
03 medical and health sciences
Hydrolysis
Protein Domains
Thioesterase
Acyl Carrier Protein
Escherichia coli
Amino Acid Sequence
chemistry.chemical_classification
biology
010405 organic chemistry
Chemistry
Fatty Acids
General Medicine
Eicosapentaenoic acid
Recombinant Proteins
0104 chemical sciences
Acyl carrier protein
030104 developmental biology
Eicosapentaenoic Acid
Palmitoyl-CoA Hydrolase
Docosahexaenoic acid
Acyltransferase
Fatty Acids, Unsaturated
biology.protein
Molecular Medicine
lipids (amino acids, peptides, and proteins)
Polyunsaturated fatty acid
- Language
- ISSN
- 1554-8937
1554-8929
Marine microorganisms de novo biosynthesize polyunsaturated fatty acids such as docosahexaenoic acid and eicosapentaenoic acid by polyunsaturated fatty acid (PUFA) synthases composed of three or four polypeptides in a manner similar to fatty acid synthases (FASs). FASs usually possess thioesterase (TE) domains to release free fatty acids from acyl carrier protein (ACP)-tethered intermediates. Here, we investigated the off-loading mechanism with microalgal and bacterial PUFA synthases through in vivo and in vitro experiments. The in vitro experiments with acyltransferase (AT)-like domains and acyl-ACP substrates clearly demonstrated that the AT-like domains catalyzed the hydrolysis of acyl-ACPs to yield free fatty acids.