A metal-independent hydrolase from a Penicillium oxalicum strain able to use phosphonoacetic acid as the only phosphorus source.
A Penicillium oxalicum strain was capable of the phosphate-sensitive utilization of phosphonoacetic acid as the sole source of phosphorus. A carbon-to-phosphorus bond-cleavage enzyme yielding acetic acid and inorganic phosphate was detected and characterized in extracts from cells grown on this phosphonate. Contrary to bacterial phosphonoacetate hydrolases, the fungal enzyme neither required nor was stimulated by divalent cations.
Klimek-Ochab
Magdalena
M
Institute of Organic Chemistry, Biochemistry and Biotechnology, Wroclaw University of Technology, PL-50370, Wroclaw, Poland. klimek@kchf.ch.pwr.wroc.pl
Lejczak
Barbara
B
Forlani
Giuseppe
G
D000469:Alkaline Phosphatase; D002244:Carbon / Q000378:metabolism; D002413:Cations, Divalent / Q000378:metabolism; D008670:Metals; D010407:Penicillium / Q000201:enzymology*; D010746:Phosphonoacetic Acid / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis / Q000378:metabolism*; D010758:Phosphorus / Q000378:metabolism*
D002413:Cations, Divalent; D008670:Metals; D010758:Phosphorus; D002244:Carbon; D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; C097254:phosphonoacetate hydrolase; D010746:Phosphonoacetic Acid