scholarly journals Farnesyl diphosphate synthase; regulation of product specificity.

2005 ◽  
Vol 52 (1) ◽  
pp. 45-55 ◽  
Author(s):  
Anna Szkopińska ◽  
Danuta Płochocka
Keyword(s):  
Environmental Changes ◽  
Gene Families ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Type I ◽  
Isopentenyl Diphosphate ◽  
Product Specificity ◽  
Dimethylallyl Diphosphate ◽  
Key Enzyme ◽  
Synthase Regulation

Farnesyl diphosphate synthase (FPPS) is a key enzyme in isoprenoid biosynthesis which supplies sesquiterpene precursors for several classes of essential metabolites including sterols, dolichols, ubiquinones and carotenoids as well as substrates for farnesylation and geranylgeranylation of proteins. It catalyzes the sequential head-to-tail condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate. The enzyme is a homodimer of subunits, typically having two aspartate-rich motifs with two sets of substrate binding sites for an allylic diphosphate and isopentenyl diphosphate per homodimer. The synthase amino-acid residues at the 4th and 5th positions before the first aspartate rich motif mainly determine product specificity. Hypothetically, type I (eukaryotic) and type II (eubacterial) FPPSs evolved from archeal geranylgeranyl diphosphate synthase by substitutions in the chain length determination region. FPPS belongs to enzymes encoded by gene families. In plants this offers the possibility of differential regulation in response to environmental changes or to herbivore or pathogen attack.

scholarly journals Improved Squalene Production via Modulation of the Methylerythritol 4-Phosphate Pathway and Heterologous Expression of Genes from Streptomyces peucetius ATCC 27952 in Escherichia coli

2009 ◽  
Vol 75 (22) ◽  
pp. 7291-7293 ◽  
Author(s):  
Gopal Prasad Ghimire ◽  
Hei Chan Lee ◽  
Jae Kyung Sohng
Keyword(s):  
Escherichia Coli ◽  
Heterologous Expression ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Streptomyces Peucetius ◽  
E Coli ◽  
Expression Of Genes ◽  
Genes Encoding

ABSTRACT Putative hopanoid genes from Streptomyces peucetius were introduced into Escherichia coli to improve the production of squalene, an industrially important compound. High expression of hopA and hopB (encoding squalene/phytoene synthases) together with hopD (encoding farnesyl diphosphate synthase) yielded 4.1 mg/liter of squalene. This level was elevated to 11.8 mg/liter when there was also increased expression of dxs and idi, E. coli genes encoding 1-deoxy-d-xylulose 5-phosphate synthase and isopentenyl diphosphate isomerase.

Farnesyl Diphosphate Synthase Reactions with Dimethylallyl Diphosphate Analogues Having Oxygen Atoms in Their Chains

1995 ◽  
Vol 24 (5) ◽  
pp. 389-390 ◽  
Author(s):  
Yuji Maki ◽  
Masayo Kurihara ◽  
Takae Endo ◽  
Megumi Abiko ◽  
Kazuhiro Saito ◽  
...  
Keyword(s):  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Dimethylallyl Diphosphate ◽  
Oxygen Atoms

scholarly journals Isolation and characterization of a gene encoding farnesyl diphosphate synthase from \(\textit{Panax vietnamensis}\) Ha et Grushv

2021 ◽  
Vol 43 (4) ◽  
pp. 119-128
Author(s):  
Nguyen Van Giang ◽  
Luu Han Ly ◽  
Pham Le Bich Hang ◽  
Le Thi Thu Hien
Keyword(s):  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
Reading Frame ◽  
Ginsenoside Biosynthesis ◽  
Isolation And Characterization ◽  
Key Enzyme ◽  
As Stress ◽  
Root Tissues

Panax vietnamensis Ha et Grushv. is a species of the genus Panax native to Central Vietnam, containing a family of triterpene saponins named ginsenosides. This group of biomolecules possesses valuable therapeutic properties against cancer, hepatitis, diabetes, inflammation as well as stress and anxiety. Farnesyl diphosphate synthase (FPS) is a key enzyme participating in the ginsenoside biosynthesis pathway. In this study, a FPS gene from P. vietnamensis (PvFPS) was isolated and characterized. The PvFPS cDNA contained an open reading frame of 1032 bp, encoding a polypeptide chain of 342 amino acid residues. Nucleotide sequence comparison showed that FPS was highly conserved among most species, with two Aspartate-rich motifs responsible for product chain length determination strongly sustained. PvFPS was closely related to those of the same genera and order and differed from those from other kingdoms. PvFPS expression was detected at a greater level in root tissues than in leaves in all ages. Our findings provided information concerning the properties of a crucial gene in the ginsenoside biosynthesis, thus enhancing our understanding of this important pathway.

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