l-lysinamidase from Cryptococcus laurenti 112. Purification and properties |
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Institution: | 1. School of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-ku, Kawasaki, Kanagawa 214-8571, Japan;2. euglena Co., Ltd., 5-29-11 Shiba Minato-ku, Tokyo 108-0014, Japan;3. RIKEN, 1-7-22, Suehirocho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan |
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Abstract: | - 1.1. The purified enzyme hydrolyzes the linear l-lysinamide and the cycle amide of l-lysine—l-α-amino-?-caprolactam.
- 2.2. The apparent relative molecular mass is 180,000. The enzyme consists of four subunits and the molecular mass of a single subunit was found to be 47,000.
- 3.3. The coefficient of molecular sedimentation equals 8.3 S, the isoelectric point was determined to be pH 4.3
- 4.4. The enzyme is not a glycoprotein. p-Mercuribenzoate binds 10 SH-groups of the native enzyme molecule and 20 SH-groups in the presence of 0.7% SDS.
- 5.5. pH- optimum for the hydrolysis of l-lysine amides was observed to be 7.5–7.7. The enzyme is strictly dependent on Mn2+ and Mg2+.
- 6.6. The kinetic parameters for the hydrolysis of l-lysinamide where Km = 3.8 mM and kcat = 3000 sec?1 For the hydrolysis of cyclic L-lysinamide Km = 4.8 mM and kcat = 2600 sec?.
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