TAILIEUCHUNG - Báo cáo khoa học: Kinetic mechanisms of glycine oxidase fromBacillus subtilis

The kinetic properties of glycine oxidase fromBacillus sub-tiliswere investigated using glycine, sarcosine, andD-proline as substrate. The turnover numbers at saturating substrate andoxygen concentrationswere s )1 , )1 , s )1 , respectively, with glycine, sarcosine, andD-proline as sub-strate. Glycine oxidase was converted to a two-electron reduced form upon anaerobic reduction with the individual substrates and its reductive half-reaction was demonstrated tobe reversible. | Eur. J. Biochem. 270 1474-1482 2003 FEBS 2003 doi Kinetic mechanisms of glycine oxidase from Bacillus subtilis Gianluca Molla Laura Motteran Viviana Job Mirella S. Pilone and Loredano Pollegioni Department of Structural and Functional Biology University of Insubria Varese Italy The kinetic properties of glycine oxidase from Bacillus sub-tilis were investigated using glycine sarcosine and D-proline as substrate. The turnover numbers at saturating substrate and oxygen concentrations were s-1 s-1 and s-1 respectively with glycine sarcosine and D-proline as substrate. Glycine oxidase was converted to a two-electron reduced form upon anaerobic reduction with the individual substrates and its reductive half-reaction was demonstrated to be reversible. The rates of flavin reduction extrapolated to saturating substrate concentration and under anaerobic conditions were 166 s-1 170 s-1 and 26 s-1 respectively with glycine sarcosine and D-proline as substrate. The rate of reoxidation of reduced glycine oxidase with oxygen in the absence of product extrapolated rate w 3 X 104 M- 1-s-1 was too slow to account for catalysis and thus reoxidation started from the reduced enzyme imino acid complex. The kinetic data are compatible with a ternary complex sequential mechanism in which the rate of product dissociation from the reoxidized enzyme form represents the rate-limiting step. Although glycine oxidase and D-amino acid oxidase differ in substrate specificity and amino acid sequence the kinetic mechanism of glycine oxidase is similar to that determined for mammalian D-amino acid oxidase on neutral D-amino acids further supporting a close similarity between these two amine oxidases. Keywords amine oxidase glycine oxidase flavoenzyme kinetic mechanism reaction mechanism. Glycine oxidase is the product of the yjbR gene of Bacillus subtilis that was predicted by sequence homology to be a flavoprotein similar to sarcosine oxidase 1 2 . Three

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