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• W2034737615 abstract "The kinetic properties of glycine oxidase from Bacillus subtilis were investigated using glycine, sarcosine, and d ‐proline as substrate. The turnover numbers at saturating substrate and oxygen concentrations were 4.0 s −1 , 4.2 s −1 , and 3.5 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 ≈ 3 × 10 4 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." @default.
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• W2034737615 date "2003-03-17" @default.
• W2034737615 modified "2023-10-17" @default.
• W2034737615 title "Kinetic mechanisms of glycine oxidase from Bacillus subtilis" @default.
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• W2034737615 doi "https://doi.org/10.1046/j.1432-1033.2003.03513.x" @default.
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