Isolation of a novel, phosphate-activated glutaminase from Bacillus pasteurii.
In Bacillus pasteurii glutamine is being taken up efficiently by a sodium-dependent uptake system and subsequently hydrolysed to ammonium and glutamate. Concerning the latter process, a catabolic L-glutamine amidohydrolase (glutaminase) was isolated from the cytoplasm of this alkaliphilic bacterium and purified to homogeneity using liquid chromatography. Biochemical and physical parameters of the pure enzyme were examined in detail. Interestingly, analysis of the glutaminase revealed a marked increase in catalytic activity in the presence of phosphate, a property yet restricted to animal glutaminases. This is the first report on the presence of a phosphate-activated glutaminase in bacteria.
Klein
Marcus
M
Institut für Medizinische, Mikrobiologie, Immunologie und Hygiene, Kliniken der Universität zu Köln, Cologne, Germany. marcus.klein@medizin.uni-koeln.de
Kaltwasser
Heinrich
H
Jahns
Thomas
T
D001407:Bacillus / Q000201:enzymology* / Q000254:growth & development; D003470:Culture Media; D004789:Enzyme Activation; D005972:Glutaminase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism; D010710:Phosphates / Q000494:pharmacology*; D013379:Substrate Specificity
D003470:Culture Media; D010710:Phosphates; D005973:Glutamine; D005972:Glutaminase