DL-α-Monofluoromethylputrescine is a potent irreversible inhibitor of Escherichia coli ornithine decarboxylase
- 15 June 1982
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 204 (3) , 771-775
- https://doi.org/10.1042/bj2040771
Abstract
DL-alpha-Monofluoromethylputrescine (compound R.M.I. 71864) is an enzyme-activated irreversible inhibitor of the biosynthetic enzyme ornithine decarboxylase from Escherichia coli. This compound, however, has much less effect in vitro on ornithine decarboxylase obtained from Pseudomonas aeruginosa. These findings are in contrast with those previously found with the substrate analogue DL-alpha-difluoromethylornithine (compound R.M.I. 71782). The K1 of the DL-alpha-monofluoromethylputrescine for the E. coli ornithine decarboxylase is 110 microM, and the half-life (t1/2) calculated for an infinite concentration of inhibitor is 2.1 min. When DL-alpha-monofluoromethylputrescine is used in combination with DL-alpha-difluoromethylarginine (R.M.I. 71897), an irreversible inhibitor of arginine decarboxylase, in vivo in E. coli, both decarboxylase activities are inhibited (greater than 95%) but putrescine levels are only decreased to about one-third of control values and spermidine levels are slightly increased.This publication has 12 references indexed in Scilit:
- Difluoromethylornithine irreversibly inactivates ornithine decarboxylase of Pseudomonas aeruginosa, but does not inhibit the enzymes of Escherichia coliBiochemical Journal, 1981
- DL-.alpha.-(Difluoromethyl)arginine: a potent enzyme-activated irreversible inhibitor of bacterial arginine decarboxylasesBiochemistry, 1981
- Irreversible inhibition of glutamate decarboxylase by .alpha.-(fluoromethyl)glutamic acidBiochemistry, 1981
- Anti-proliferative properties of DL-α-difluoromethyl ornithine in cultured cells. A consequence of the irreversible inhibition of ornithine decarboxylaseBiochemical and Biophysical Research Communications, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Catalytic inhibition of γ-aminobutyric acid-α-ketoglutarate transaminase of bacterial origin by 4-aminohex-5-ynoic acid, a substrate analogBiochemical and Biophysical Research Communications, 1975
- Chemistry and Enzymology of k cat InhibitorsScience, 1974
- Dissociation of putrescine-activated decarboxylation of S-adenosyl-L-methionine from the enzymic synthesis of spermidine and spermine by purified prostatic enzyme preparationsBiochemical and Biophysical Research Communications, 1971
- Esters of Methanesulfonic Acid as Irreversible Inhibitors of AcetylcholinesteraseJournal of Biological Chemistry, 1962
- MUTANTS OF ESCHERICHIA COLI REQUIRING METHIONINE OR VITAMIN B 12Journal of Bacteriology, 1950