Analysis and engineering of substrate shuttling by the acyl carrier protein (ACP) in fatty acid synthases (FASs)

Emanuele Rossini; Jan Gajewski; Maja Klaus; Gerhard Hummer; Martin Grininger

doi:10.1039/c8cc06838k

Analysis and engineering of substrate shuttling by the acyl carrier protein (ACP) in fatty acid synthases (FASs)

Chem Commun (Camb). 2018 Oct 11;54(82):11606-11609. doi: 10.1039/c8cc06838k.

Authors

Emanuele Rossini¹, Jan Gajewski, Maja Klaus, Gerhard Hummer, Martin Grininger

Affiliation

¹ Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany. gerhard.hummer@biophys.mpg.de.

PMID: 30264077
DOI: 10.1039/c8cc06838k

Abstract

Perturbations of domain-domain interactions impact the function of type I fatty acid synthases. We identify interface point mutations that modulate fatty acid chain lengths, and explain their effect in changes of domain-domain binding energetics. Engineering of similar interfaces in related megasynthases may be exploited for custom synthesis of natural products.

MeSH terms

Acyl Carrier Protein / chemistry
Acyl Carrier Protein / genetics
Acyl Carrier Protein / metabolism*
Amino Acid Sequence
Binding Sites
Fatty Acid Synthase, Type I / chemistry
Fatty Acid Synthase, Type I / genetics
Fatty Acid Synthase, Type I / metabolism*
Fatty Acids / chemistry
Fatty Acids / metabolism*
Molecular Docking Simulation
Point Mutation
Protein Engineering
Protein Interaction Domains and Motifs
Saccharomyces cerevisiae / chemistry
Saccharomyces cerevisiae / genetics
Saccharomyces cerevisiae / metabolism*
Saccharomyces cerevisiae Proteins / chemistry
Saccharomyces cerevisiae Proteins / genetics
Saccharomyces cerevisiae Proteins / metabolism*
Thermodynamics

Substances

Acyl Carrier Protein
Fatty Acids
Saccharomyces cerevisiae Proteins
Fatty Acid Synthase, Type I