Hernández-Jodra M, Gancedo C
Hoppe Seylers Z Physiol Chem. 1979 Apr;360(4):581-6. doi: 10.1515/bchm2.1979.360.1.581.
A carboxypeptidase has been identified in Rhodotorula glutinis and partially purified. The enzyme is active on N-substituted dipeptides and tripeptides and also exhibits an esterolytic activity. Both activities are inhibited by (N-benzyloxycarbonyl-L-phenylalanyl)chloromethane and by a thermostable fraction present in extracts. The enzyme shows a pH optimum in the range 7.5 to 8.0 and has a molecular weight of 80000, determined by gel filtration.
