The purification of 3,3-dimethylallyl- and geranyl-transferase and of isopentenyl pyrophosphate isomerase from pig liver.

Content Provider	Semantic Scholar
Author	Holloway, Peter W. Popják, George
Copyright Year	1967
Abstract	The enzyme catalysing the synthesis of farnesyl pyrophosphate from dimethylallyl pyrophosphate and isopentenyl pyrophosphate, or from geranyl pyrophosphate and isopentenyl pyrophosphate, has been purified 100-fold from homogenates of pig liver. The enzyme has optimum pH 7.9 and requires Mg(2+) as activator in preference to Mn(2+); it is inhibited by iodoacetamide, N-ethylmaleimide, p-hydroxymercuribenzoate and phosphate ions in addition to the products of the reaction, inorganic pyrophosphate and farnesyl pyrophosphate. From product-inhibition studies of the geranyltransferase reaction, the order of addition of substrates to and release of products from the enzyme has been deduced: geranyl pyrophosphate combines with the enzyme first, followed by isopentenyl pyrophosphate. Farnesyl pyrophosphate dissociates from the enzyme before inorganic pyrophosphate. The existence of isopentenyl pyrophosphate isomerase in liver is confirmed. Methods for the preparation of the pyrophosphate esters of isopentenol, 3,3-dimethylallyl alcohol, geraniol and farnesol are also described.
Starting Page	57
Ending Page	70
Page Count	14
File Format	PDF HTM / HTML
DOI	10.1042/bj1040057
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/104/1/57.full.pdf
PubMed reference number	4292002
Alternate Webpage(s)	https://doi.org/10.1042/bj1040057
Journal	Medline
Volume Number	104
Issue Number	1
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article