Mechanism of aluminium-induced porphyrin synthesis in bacteria |
| |
Authors: | Rivka Mamet Ram Scharf Yoram Zimmels Shlomo Kimchie Nili Schoenfeld |
| |
Affiliation: | (1) The Laboratory of Biochemical Pharmacology, Beilinson Medical Center, Petah Tikva, Israel;(2) The Department of Pathological Chemistry, Sackler Faculty of Medicine, University of Tel Aviv, Ramat Aviv, Israel;(3) The Department of Environmental Engineering, Technion-Israel Institute of Technology, Haifa, Israel;(4) Laboratory of Biochemical Pharmacology, Beilinson Medical Center, 49 100 Petah Tikva, Israel |
| |
Abstract: | In previous studies, aluminium was found to retard bacterial growth and enhance porphyrin formation in Arthrobacter aurescens RS-2. The aim of this study was to establish the mechanism of action of aluminium which leads to increased porphyrin production. Cultures of Arthrobacter aurescens RS-2 were incubated in the absence and presence of 0.74 mm aluminium. After 6 and 24 h of incubation, various parameters of the haem biosynthetic pathway were determined. After 6 h of incubation with aluminium, the activities of the enzymes aminolevulinate synthase (ALAS), aminolevulinate dehydratase (ALAD), porphobilinogen deaminase (PBGD) and uroporphyrinogen decarboxylase (UROD) were increased by 120, 170, 190 and 203%, respectively, while that of ferrochelatase (FC) was found to be unchanged. However, after 24 h of incubation, no change in the activities of ALAS and ALAD was noted, while an about 2-fold increase in PBGD and UROD activities were observed. FC activity was decreased by 63%. It was concluded that aluminium exerts its effect by inducing the enzymes PBGD and UROD rather than by a direct or indirect effect on ALAS. Its effect on the final step in the haem biosynthetic pathway is discussed. |
| |
Keywords: | aluminium bacteria porphobilinogen deaminase porphyrin synthesis uroporphyrinogen decarboxylase |
本文献已被 SpringerLink 等数据库收录! |
|