Article
Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the newly characterized Dlp1 protein in a novel heterotetrameric structure.
European journal of biochemistry - 1 Oct 2003
Saiki Ryoichi, Nagata Ai, Uchida Naonori, Kainou Tomohiro, Matsuda Hideyuki, Kawamukai Makoto
Abstract excerpt
The analysis of the structure and function of long chain-producing polyprenyl diphosphate synthase, which synthesizes the side chain of ubiquinone, has largely focused on the prokaryotic enzymes, and little is known about the eukaryotic counterparts. Here we show that decaprenyl diphosphate synthase from Schizosaccharomyces pombe is comprised of a novel protein named Dlp1 acting in partnership with Dps1. Dps1 is...
Topics
- Alkyl and Aryl Transferases
- Amino Acid Sequence
- Cloning, Molecular
- Molecular Sequence Data
- Phenotype
- Protein Structure, Quaternary
- Schizosaccharomyces
- Sequence Alignment
- Ubiquinone