Table 3.

Substrate specificity of wild‐type and D238F mutant enzymes of l‐AAO/MOG

Substratea	Wild‐type		D238F
	0.1 mm	5 mm	0.1 mm	5 mm
l‐Lys	0.26 ± 0.05	0.53 ± 0.04	0.059 ± 0.01	0.13 ± 0.01
l‐Orn	0.28 ± 0.01	0.13 ± 0.02	0.009 ± 0.0002	0.0025 ± 0.0001
l‐Arg	0.11 ± 0.008	0.11 ± 0.01	0.011 ± 0.001	0.11 ± 0.01
l‐Ala	−b	−b	0.012 ± 0.0005	0.0085 ± 0.0005
l‐Leu	−b	−b	0.024 ± 0.003	0.38 ± 0.03
l‐Phe	−b	−b	0.010 ± 0.002	0.055 ± 0.005
l‐Met	−b	−b	0.011 ± 0.008	0.23 ± 0.01
Cadaverine	−b	−b	0.021 ± 0.001	0.0119 ± 0.0004

Oxidase activity (units·mg⁻¹) against 23 amino acid substrates (0.1 or 5 mm) was measured (n = 3) at pH 7.0 and 30 °C as described in Materials and methods. ^a Both enzymes showed no activity to l‐His, l‐Ser, l‐Thr, l‐Asn, l‐Gln, l‐Asp, l‐Glu, Gly, l‐Val, l‐Ile, l‐Tyr, l‐Trp, l‐Cys, l‐Pro, d‐Lys, d‐Orn, and d‐Arg. ^b Not detected.