Article
Substrate and product binding sites of yeast fatty acid synthase. Stoichiometry and binding kinetics of wild-type and in vitro mutated enzymes.
European journal of biochemistry - 1 Mar 1995
Schuster H, Rautenstrauss B, Mittag M, Stratmann D, Schweizer E
Abstract excerpt
The four known substrate binding sites of yeast fatty acid synthase (FAS), Ser819 (acetyltransferase, OHAC) and Ser5421 (malonyl/palmitoyl transferase, OHMa1) of subunit beta and Ser180 (pantetheine binding site, SHc) and Cys1305 (3-oxoacyl synthase, SHp) of subunit alpha were replaced, by targeted in vitro mutagenesis, by the non-acylatable amino acids glutamine, glycine or alanine. The four mutated FAS proteins...
Topics
- Acetates
- Acetic Acid
- Acylation
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Fatty Acid Synthases
- Fatty Acids
- Malonates
- Molecular Sequence Data
- Mutation