Polyphosphate-dependent enzymes in some coryneform bacteria isolated from sewage sludge.
Eleven isolates obtained from a laboratory sewage treatment plant, most of them presumptively assigned to the coryneform genera Curtobacterium and Aureobacterium were studied for the presence of intracellular polyphosphates and polyphosphate dependent enzymes. All isolates stored polyphosphates and showed adenylate kinase activities ranging from 64 to 815 mU mg-1. Polyphosphate:AMP phosphotransferase could only be detected in one isolate. Three isolates showed a polyphosphate kinase activity also in minor amounts from 15 to 17 mU mg-1. A polyphosphate dependent NAD or 3-phosphoglycerate kinase could not be detected. Polyphosphate glucokinase activity was measured in cell-free extracts of nine isolates ranging from 2 to 376 mU mg-1. Three isolates showed in addition to the polyphosphate glucokinase, a glucose-6-phosphate-dependent NAD kinase. For the regeneration of NADP from NAD and polyphosphate, this enzyme system may give the isolates a distinct competitive advantage, especially for anabolic processes. The polyphosphate-dependent enzymes reported here may play an additional role in the complex process of 'biological' phosphate removal from wastewater.
Fachgebiet Hygiene, Technische Universität Berlin, FRG.
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D000192:Actinomycetales / Q000201:enzymology / Q000302:isolation & purification / Q000378:metabolism*; D010770:Phosphotransferases / Q000378:metabolism; D017853:Phosphotransferases (Alcohol Group Acceptor); D011122:Polyphosphates / Q000378:metabolism*; D012722:Sewage
D011122:Polyphosphates; D012722:Sewage; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C021844:NAD kinase; C024812:polyphosphate-glucose phosphotransferase