GALLERT, C and WINTER, J (1992) COMPARISON OF 4-HYDROXYBENZOATE DECARBOXYLASE AND PHENOL CARBOXYLASE ACTIVITIES IN CELL-FREE-EXTRACTS OF A DEFINED, 4-HYDROXYBENZOATE AND PHENOL-DEGRADING ANAEROBIC CONSORTIUM. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 37 (1). pp. 119-124. ISSN 0175-7598,
Full text not available from this repository.Abstract
Two 4-hydroxybenzoate decarboxylase activities and a phenol carboxylase activity were found in cell-free extracts of a defined, 4-hydroxybenzoate- or phenol-grown consortium. Both decarboxylase activities were loosely membrane-associated and required K+ but a different pH and ion strength. Loss of activity of both decarboxylases by EDTA could be compensated by Zn2+ ions. The K(m) values for 4-hydroxybenzoate and K+ of the decarboxylase activities with pH optima at 6.4 or 7.8 were 0.02 and 2.5 or 0.004 and 0.5 mm, respectively. 3,4-Dihydroxybenzoate, 3,4,5-trihydroxybenzoate, 3,5-dimethoxy-4-hydroxybenzoate and 3-chloro-4-hydroxybenzoate were also decarboxylated by both enzyme activities. The phenol carboxylase was a soluble enzyme with its pH optimum at 6.5. It required K+, Rb+ or NH4+ as monovalent, Zn2+, Mg2+, Mn2+ or Ni2+ as divalent cations and catalysed the carboxylation of phenol if 2,4-, 2,3,4- or 2,4,6-hydroxybenzoates were absent. The three enzyme activities were not influenced by Avidin and thus were probably not biotin-dependent enzymes.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DEGRADATION; BENZOATE; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:44 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54578 |
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