ChemInform Abstract: Substrate Specificity of Thermostable Farnesyl Diphosphate Synthase with Alkyl Group Homologues of Isopentenyl Diphosphate.

ChemInform ◽  
2010 ◽  
Vol 30 (3) ◽  
pp. no-no
Author(s):  
M. NAGAKI ◽  
H. KANNARI ◽  
J. ISHIBASHI ◽  
Y. MAKI ◽  
T. NISHINO ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Alkyl Group ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Isopentenyl Diphosphate

Substrate specificity of thermostable farnesyl diphosphate synthase with alkyl group homologs of isopentenyl diphosphate

1998 ◽  
Vol 8 (18) ◽  
pp. 2549-2554 ◽  
Author(s):  
Masahiko Nagaki ◽  
Hiroki Kannari ◽  
Junji Ishibashi ◽  
Yuji Maki ◽  
Tokuzo Nishino ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Alkyl Group ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase ◽  
Isopentenyl Diphosphate

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.

Substrate specificity of farnesyl diphosphate synthase from Bacillus stearothermophilus

1995 ◽  
Vol 5 (15) ◽  
pp. 1605-1608 ◽  
Author(s):  
Yuji Maki ◽  
Akiko Masukawa ◽  
Hideaki Ono ◽  
Takae Endo ◽  
Tanetoshi Koyama ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Bacillus Stearothermophilus ◽  
Farnesyl Diphosphate ◽  
Farnesyl Diphosphate Synthase
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