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Enzymatic Aspects of Isoprenoid Chain Elongation.
Molecular cloning, expression and characterization of cDNA encoding cis-prenyltransferases from Hevea brasiliensis. A key factor participating in natural rubber biosynthesis.
- Kasem Asawatreratanakul, Yuan-Wei Zhang, T. Koyama
- BiologyEuropean journal of biochemistry
- 1 December 2003
In vitro rubber transferase assays using the recombinant gene product overexpressed in Escherichia coli revealed that the enzyme catalyzed the formation of long chain polyprenyl products with approximate sizes of 2 x 103-1 x 104 Da, suggesting that the Hevea cis-prenytransferase might require certain activation factors in the washed bottom fraction particles for the production of high molecular mass rubber.
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
- M. Fujihashi, Y. W. Zhang, Y. Higuchi, X. Y. Li, T. Koyama, K. Miki
- ChemistryProceedings of the National Academy of Sciences…
- 3 April 2001
The crystal structure of UPS is reported as the only three-dimensional structure among cis-prenyl chain elongating enzymes and is classified into a protein fold family and is completely different from the so-called “isoprenoid synthase fold” that is believed to be a common structure for the enzymes relating to isoprenoids biosynthesis.
Conversion from Farnesyl Diphosphate Synthase to Geranylgeranyl Diphosphate Synthase by Random Chemical Mutagenesis (*)
- S. Ohnuma, Takeshi Nakazawa, T. Nishino
- Chemistry, BiologyThe Journal of Biological Chemistry
- 26 April 1996
Comparisons of kinetic parameters of the mutated and wild type enzymes revealed several phenomena that may relate with the change of the ultimate chain length, which might suggest that the aromatic ring of tyrosine 81 blocks the chain elongation longer than FPP.
Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification.
The structural gene for thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus was cloned, sequenced, and overexpressed in Escherichia coli cells and the deduced amino acid sequence shows a 42% similarity with that of E. coli FPP synthase.
KaPPA-View. A Web-Based Analysis Tool for Integration of Transcript and Metabolite Data on Plant Metabolic Pathway Maps1[w]
A Web-based tool, KaPPA-View, for representing quantitative data for individual transcripts and/or metabolites on plant metabolic pathway maps, and describes the dataset obtained for transgenic plants that overexpress the PAP1 gene encoding a MYB transcription factor on metabolic pathways maps.
Structure and function of cis-prenyl chain elongating enzymes.
Comparison of the structures of short, medium, and long-chain cis-prenyltransferases reveals important amino acid residues for product chain length determination, which enabled us to understand the regulation mechanism of the ultimate chain length among cis- prenyl transferases.
Molecular analysis of cis-prenyl chain elongating enzymes.
This review covers up to February 2002 and contains 72 references and reveals that the primary structure but also the crystal structure of the cis-prenyltransferase is totally different from those of trans- prenyl chain elongating enzymes.
Manipulation of prenyl chain length determination mechanism of cis‐prenyltransferases
- Y. Kharel, Seiji Takahashi, S. Yamashita, T. Koyama
- Biology, ChemistryThe FEBS journal
- 1 February 2006
It is reported here that the ultimate chain length of prenyl products can be controlled through structural manipulation of UPP synthase of M.’luteus B‐P 26, based on comparisons between structures of various cis‐prenyltransferases.
Molecular analysis of prenyl chain elongating enzymes.
- T. Koyama
- Biology, ChemistryBioscience, biotechnology, and biochemistry
Protein data base searches for sequences similar to that of the undecaprenyl diphosphate synthase yielded many unknown proteins which have not yet been characterized, indicating that there are three highly conserved regions in the primary structure of (Z)-prenyl chain elongating enzymes.