Partial purification and properties of gamma-glutamyltranspeptidase from mycelia of Morchella esculenta.

Three gamma-glutamyltranspeptidase (enzymes I, II and III) were partially purified from the cell free extracts of the cultured mycelia of Morchella esculenta Fr. The molecular masses of enzymes were 155,000 (I), 219,000 (II) and 102,000 (III). All of them catalyzed both hydrolysis and transpeptidation of various gamma-glutamyl compounds. gamma-L-Glutamyl-cis-3-amino-L-proline occurring in the cultured mycelia of this fungus was a good substrate for both reactions. Km values for hydrolysis were in the order of 10(-4) to 10(-5) M, and those for transpeptidation were in the order of 10(-2) to 10(-4) M. The enzymes were inhibited by a gamma-glutamyltranspeptidase inhibitor, L-serine plus borate.