Strain Pseudomonas Aeraginosa SCU isolated from rotten hides is shown to produce various gelatinolytic enzymes with molecular masses ranging from ～50 to ～200 kD. A gelatinolytic enzyme called PAC exhibiting collagenolytic activity is purified by SP sepharose fast flow, Sephadex G-200 gel filtration and native PAGE cutting method. The purified enzyme has an apparent molecular weight of about 110 kD by SDS PAGE without β-mercaptoethanol. Treatment withβ-Me suggests that PAC is dissociated into three subunits approximately 33 kD,25 kD and 20 kD with a ratio of 2∶1∶1, named sub A, sub B and sub C repectively. EDTA and EGTA display a significant inhibitory effect on the enzyme activity while PMSF, leupeptin and pepstain do not appreciably inhibit it. The first 15 amino acid residues of the major subunit (subA) are determined and the sequence is Ala-Glu-Ala-Gly-Gly-Pro-Gly-Gly-Asn-Gln-Lys-Ile-Gly -Lys-Tyr. This sequence is identical to that of elastase of P.aeruginosa. The fragment of encoding mature sub A is cloned and its sequence is determined, which has a high homology with the gene of elastase. These results indicate that PAC is a novel collagenolytic metalloprotease composed of three kinds of subunits, of which elastase is the major one.