EC Number |
Title |
Organism |
---|
3.4.24.40 | Biochemical and functional characterization of a metalloprotease from the thermophilic fungus Thermoascus aurantiacus |
Thermoascus aurantiacus |
3.4.24.40 | Characterization of arazyme, an exocellular metalloprotease isolated from Serratia proteamaculans culture medium |
Serratia proteamaculans |
3.4.24.40 | A fibrinolytic, alkaline and thermostable metalloprotease from the newly isolated Serratia sp RSPB11 |
Serratia marcescens |
3.4.24.40 | A fibrinolytic, alkaline and thermostable metalloprotease from the newly isolated Serratia sp RSPB11 |
Serratia marcescens RSPB11 |
3.4.24.40 | A new broad specificity alkaline metalloprotease from a Pseudomonas sp. isolated from refrigerated milk: Role of calcium in improving enzyme productivity |
Pseudomonas sp. |
3.4.24.40 | A new broad specificity alkaline metalloprotease from a Pseudomonas sp. isolated from refrigerated milk: Role of calcium in improving enzyme productivity |
Pseudomonas sp. RC |
3.4.24.40 | A novel serralysin metalloprotease from Deinococcus radiodurans |
Deinococcus radiodurans |
3.4.24.40 | Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases |
Pseudomonas aeruginosa |
3.4.24.40 | Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins |
Dickeya chrysanthemi |
3.4.24.40 | Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins |
Pseudomonas aeruginosa |