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Updated: Aug 6, 2026
07:35
Overexpression and Purification of Human Cis-prenyltransferase in Escherichia coli
Published on: August 3, 2017
Structure and function of cis-prenyl chain elongating enzymes
Seiji Takahashi1, Tanetoshi Koyama
1Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan.
Chemical Record (New York, N.Y.)
|August 11, 2006
Summary
This study details the structure and catalytic mechanisms of cis-prenyltransferases, enzymes crucial for isoprenoid synthesis. Researchers elucidated key amino acid residues involved in determining product chain length for these essential biological catalysts.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Isoprenoids, vital molecules with diverse chain lengths, are synthesized by prenyltransferases.
- Prenyltransferases are classified as trans- or cis- types based on product geometry.
- While trans-prenyltransferases are well-studied, cis-prenyltransferase mechanisms remained largely unknown until recently.
Purpose of the Study:
- To elucidate the structure and catalytic mechanisms of cis-prenyltransferases.
- To identify conserved regions and key amino acid residues in cis-prenyltransferases.
- To understand the regulation of product chain length determination in cis-prenyltransferases.
Main Methods:
- Gene identification and cloning of undecaprenyl diphosphate (UPP) synthase.
- Determination of UPP synthase primary and tertiary structures.
- Site-directed mutagenesis of conserved amino acid residues in UPP synthases.
- Comparative structural analysis of short-, medium-, and long-chain cis-prenyltransferases.
Main Results:
- The structure of cis-prenyltransferases, exemplified by UPP synthase, differs significantly from trans-prenyltransferases.
- Five highly conserved regions were identified across various cis-prenyltransferases.
- Site-directed mutagenesis revealed the catalytic mechanisms and identified residues critical for controlling isoprenoid chain length.
Conclusions:
- The study provides the first detailed structural and mechanistic insights into cis-prenyltransferases.
- Understanding these enzymes is key to comprehending the biosynthesis of a wide range of isoprenoids.
- Identification of chain length-determining residues opens avenues for enzyme engineering and synthetic biology applications.
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