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Purification and properties of agmatine amidinohydrolase of Evernia prunastri
Author(s) -
Vicente C.,
Legaz María Estrella
Publication year - 1982
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1982.tb00301.x
Subject(s) - agmatine , chemistry , putrescine , biochemistry , enzyme , urea , substrate (aquarium) , arginine , chromatography , biology , amino acid , ecology
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 K m for agmatine was estimated to be 6.4 m M .