Purification and properties of agmatine amidinohydrolase of Evernia prunastri |
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Authors: | C Vicente María Estrella Legaz |
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Institution: | Dept. of Plant Physiology, The Lichen Team, Faculty of Biology, Complutense Univ., Madrid -3-, Spain. |
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Abstract: | An agmatine amidinohydrolase (EC 3.5.3.11) has been purified from Evernia prunastri (L.) Ach. thallus incubated on 40 m M L-arginine at 26°C in the dark. The enzyme was purified 485-fold with an overall yield of 55%. It shows a pH optimum of 6.9, a temperature optimum at 35–40°C and a molecular mass (weight) of about 320 000. The Evernia hydrolase is significantly activated by L-arginine, L-ornithine and putrescine for agmatine concentrations lower than 14 m M and inhibited for agmatine concentrations producing inhibition by an excess of substrate. Urea was always a powerful inhibitor of the enzyme. The Km for agmatine was estimated to be 6.4 m M . |
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Keywords: | L-arginine enzyme purification L-ornithine putrescine urea |
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