Structure and Mechanism of the Ketosynthase-Chain Length Factor Didomain from a Prototypical Polyunsaturated Fatty Acid Synthase.
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Biosynthetic Pathways
Catalytic Domain
/ genetics
Crystallography, X-Ray
Fatty Acid Synthase, Type II
/ chemistry
Fatty Acids, Unsaturated
/ biosynthesis
Humans
Mass Spectrometry
Models, Molecular
Moritella
/ enzymology
Mutagenesis, Site-Directed
Protein Domains
Recombinant Proteins
/ chemistry
Sequence Homology, Amino Acid
Static Electricity
Substrate Specificity
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
22 12 2020
22 12 2020
Historique:
pubmed:
8
12
2020
medline:
7
4
2021
entrez:
7
12
2020
Statut:
ppublish
Résumé
Long-chain polyunsaturated fatty acids (LC-PUFAs) are essential ingredients of the human diet. They are synthesized by LC-PUFA synthases (PFASs) expressed in marine bacteria and other organisms. PFASs are large enzyme complexes that are homologous to mammalian fatty acid synthases and microbial polyketide synthases. One subunit of each PFAS harbors consecutive ketosynthase (KSc) and chain length factor (CLF) domains that collectively catalyze the elongation of a nascent fatty acyl chain via iterative carbon-carbon bond formation. We report the X-ray crystal structure of the KS-CLF didomain from a well-studied PFAS in
Identifiants
pubmed: 33283513
doi: 10.1021/acs.biochem.0c00785
doi:
Substances chimiques
Bacterial Proteins
0
Fatty Acids, Unsaturated
0
Recombinant Proteins
0
Fatty Acid Synthase, Type II
EC 6.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4735-4743Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM087934
Pays : United States