Prenyl Alcohol Production by Expression of Exogenous Isopentenyl Diphosphate Isomerase and Farnesyl Diphosphate Synthase Genes inEscherichia coli

2009 ◽  
Vol 73 (1) ◽  
pp. 186-188 ◽  
Author(s):  
Chikara OHTO ◽  
Masayoshi MURAMATSU ◽  
Shusei OBATA ◽  
Eiji SAKURADANI ◽  
Sakayu SHIMIZU
Keyword(s):  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Isopentenyl Diphosphate ◽  
Inescherichia Coli ◽  
Isopentenyl Diphosphate Isomerase ◽  
Alcohol Production

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.

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 Purification, Enzymatic Characterization, and Inhibition of theZ-Farnesyl Diphosphate Synthase fromMycobacterium tuberculosis

2001 ◽  
Vol 276 (15) ◽  
pp. 11624-11630 ◽  
Author(s):  
Mark C. Schulbach ◽  
Sebabrata Mahapatra ◽  
Marco Macchia ◽  
Silvia Barontini ◽  
Chiara Papi ◽  
...  
Keyword(s):  
Expression System ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Isopentenyl Diphosphate ◽  
Enzymatic Characterization ◽  
Geranyl Diphosphate ◽  
Reading Frame ◽  
Absolute Requirement ◽  
Ph Range ◽  
Mycobacterial Cell Wall

We have recently shown that open reading frame Rv1086 of theMycobacterium tuberculosisH37Rv genome sequence encodes a unique isoprenyl diphosphate synthase. The product of this enzyme,ω,E,Z-farnesyl diphosphate, is an intermediate for the synthesis of decaprenyl phosphate, which has a central role in the biosynthesis of most features of the mycobacterial cell wall, including peptidoglycan, arabinan, linker unit galactan, and lipoarabinomannan. We have now purifiedZ-farnesyl diphosphate synthase to near homogeneity using a novel mycobacterial expression system.Z-Farnesyl diphosphate synthase catalyzed the addition of isopentenyl diphosphate toω,E-geranyl diphosphate orω,Z-neryl diphosphate yieldingω,E,Z-farnesyl diphosphate andω,Z,Z-farnesyl diphosphate, respectively. The enzyme has an absolute requirement for a divalent cation, an optimal pH range of 7–8, andKmvalues of 124 μmfor isopentenyl diphosphate, 38 μmfor geranyl diphosphate, and 16 μmfor neryl diphosphate. Inhibitors of theZ-farnesyl diphosphate synthase were designed and chemically synthesized as stable analogs ofω,E-geranyl diphosphate in which the labile diphosphate moiety was replaced with stable moieties. Studies with these compounds revealed that the active site ofZ-farnesyl diphosphate synthase differs substantially fromE-farnesyl diphosphate synthase from pig brain (Sus scrofa).

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