Isolation, Purification, and Characterization of a New Enzyme from Pseudomonas sp. M-27,Carboxypeptidase G_3

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A new type of carboxypeptidase was found in a strain of Pseudomonas sp. M-27 isolated from soil. The cell-free extract, solubilized by colistin sulfate, was purified to homogeneity. This enzyme had a single peak with a molecular weight of 60,000 on a calibrated Superdex column and consisted of four subunits of identical molecular weights (M_r : 15,000). The enzyme hydrolyzed predominately acidic peptides and N-acyl amino acids with Glu or Asp in the C-termini. This enzyme was not strongly affected by thiol enzyme inhibitors (PCMB, iodoacetic acid) or serine protease inhibitors (DFP, PMSF), but was inhibited by metal chelators. The enzyme resembles resembles carboxypeptidase G_1 or G_2 in its glutamate-releasing activity. However, it acts not noly on the L-form but also on the D-form of acidic amino acids and shows affinity for the long-chain fatty acyl group but not the benzoyl group. Thus, as this enzyme differs from carboxypeptidase G_1 or G_2,it was named carboxypeptidase G_3.
社団法人日本農芸化学会の論文
1992-10-23