Identification of the polyamine N 8-acetyltransferase involved in the pathway of 1,3-diaminopropane production in Acanthamoeba culbertsoni |
| |
Authors: | Onkar P. Shukla Siaka O. Aisien Bärbel Bergmann Claudia Hellmund R. D. Walter |
| |
Affiliation: | (1) Division of Biochemistry, Central Drug Research Institute, Lucknow, India, IN;(2) Department of Biochemical Parasitology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Strasse 74, D-20359 Hamburg, Germany, DE |
| |
Abstract: | A cytosolic polyamine N-acetyltransferase that preferentially catalyzes the acetylation of spermidine in the N 8-position was identified in the free-living pathogenic amoeba Acanthamoeba culbertsoni. In addition to spermidine, the enzyme also catalyzed the acetylation of spermine and putrescine with Michaelis constants (K m values) of 97, 12, and 10 μM, respectively. The K m value for acetylcoenzyme A (acetyl-CoA) was estimated to be 11 μM, whereas CoA had an inhibitory constant of 6 μM. The N-acetylase has a molecular mass of approximately 45 kDa. That the enzyme preferentially catalyzed the acetylation of spermidine at the N 8-position, resulting in N 8-acetylspermidine, the preferred substrate of the polyamine oxidase found in A. culbertsoni, indicates a role for the enzyme in the production of 1,3-diaminopropane, the major polyamine found in the Acanthamoeba. Received: 20 June 1995 / Accepted: 16 September 1995 |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|