Isobutylidenediurea degradation by Rhodococcus erythropolis.
A new enzyme (isobutylidenediurea amidinohydrolase) catalyzing the hydrolysis of isobutylidenediurea (a condensation product of urea and isobutyraldehyde widely used as a slow-release nitrogeneous fertilizer) was characterized from a strain of Rhodococcus erythropolis. The enzyme was purified 1,250-fold to apparent homogeneity and shown to hydrolyze the fertilizer to urea and isobutyraldehyde at a molar ratio of 2: 1. No activity was observed with ureido- or other structurally related compounds. Its molecular mass was determined by native polyacrylamide gelelectrophoresis and matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry to be 15 kDa (+/-2 kDa) and 16.4 kDa, respectively. Growth of the bacterium in the presence of isobutylidenediurea led to an increased expression of the constitutively synthetized enzyme.
Jahns
T
T
Fachrichtung 8.3 Mikrobiologie, Universität des Saarlandes, Saarbrücken, FRG. toja@mx.uni-saarland.de
Schepp
R
R
D001673:Biodegradation, Environmental; D001736:Biureas / Q000032:analysis / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005308:Fertilizers / Q000032:analysis*; D006868:Hydrolysis; D007202:Indicators and Reagents; D008970:Molecular Weight; D015203:Reproducibility of Results; D012240:Rhodococcus / Q000378:metabolism*; D012988:Soil Microbiology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013379:Substrate Specificity
D001736:Biureas; D005308:Fertilizers; D007202:Indicators and Reagents; C014058:isobutylidene diurea