EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.37 | iodoacetate | 11% activation at 1 mM | Debaryomyces hansenii |
EC Number | Application | Comment | Organism |
---|---|---|---|
3.4.23.25 | food industry | possibly involved in ripening processes of fermented meat products | Debaryomyces hansenii |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.23.25 | 2-mercaptoethanol | - |
Debaryomyces hansenii | |
3.4.23.25 | DTT | - |
Debaryomyces hansenii | |
3.4.23.25 | HgCl2 | complete inhibition at 0.05 mM | Debaryomyces hansenii | |
3.4.23.25 | iodoacetate | weak inhibitor | Debaryomyces hansenii | |
3.4.23.25 | leupeptin | strong inhibitor | Debaryomyces hansenii | |
3.4.23.25 | p-chloromercuribenzoic acid | complete inhibition at 0.1 mM | Debaryomyces hansenii | |
3.4.23.25 | pepstatin A | - |
Debaryomyces hansenii | |
3.4.23.25 | PMSF | weak inhibitor | Debaryomyces hansenii | |
3.4.24.37 | 1,10-phenanthroline | complete inhibition at 0.1 mM | Debaryomyces hansenii | |
3.4.24.37 | 2-mercaptoethanol | 19% inhibition at 5 mM | Debaryomyces hansenii | |
3.4.24.37 | 3,4-dichloroisocoumarin | 71% inhibition at 1 mM | Debaryomyces hansenii | |
3.4.24.37 | 4-chloromercuribenzoate | complete inhibition at 0.1 mM | Debaryomyces hansenii | |
3.4.24.37 | Cd2+ | 33% inhibition at 0.5 mM | Debaryomyces hansenii | |
3.4.24.37 | DTT | 19% inhibition at 1 mM | Debaryomyces hansenii | |
3.4.24.37 | EGTA | 35% inhibition at 5 mM | Debaryomyces hansenii | |
3.4.24.37 | Hg2+ | complete inhibition at 0.05 mM | Debaryomyces hansenii | |
3.4.24.37 | Mg2+ | 21% inhibition at 0.5 mM | Debaryomyces hansenii | |
3.4.24.37 | additional information | no inhibition by EDTA at 5 mM | Debaryomyces hansenii | |
3.4.24.37 | pepstatin A | 15% inhibition at 1 mM | Debaryomyces hansenii | |
3.4.24.37 | PMSF | 50% inhibition at 1 mM | Debaryomyces hansenii | |
3.4.24.37 | Zn2+ | 73% inhibition at 0.5 mM | Debaryomyces hansenii |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.37 | additional information | metalloprotease, not affeted by Cu2+, Co2+, Mn2+, and Ca2+ | Debaryomyces hansenii |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.23.25 | 42000 | - |
1 * 42000, SDS-PAGE, native mass by gel filtration | Debaryomyces hansenii |
3.4.23.25 | 55000 | - |
gel filtration | Debaryomyces hansenii |
3.4.24.37 | 65000 | - |
1 * 65000, SDS-PAGE | Debaryomyces hansenii |
3.4.24.37 | 68000 | - |
gel filtration | Debaryomyces hansenii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.23.25 | Debaryomyces hansenii | - |
- |
- |
3.4.23.25 | Debaryomyces hansenii CECT12487 | - |
- |
- |
3.4.24.37 | Debaryomyces hansenii | - |
isolated from the natural microflora of fermented sausages and selected as possible starter culture on the basis of its physiological and biochemical properties and its ability to compete during sausage manufacturing processes | - |
3.4.24.37 | Debaryomyces hansenii CECT 12487 | - |
isolated from the natural microflora of fermented sausages and selected as possible starter culture on the basis of its physiological and biochemical properties and its ability to compete during sausage manufacturing processes | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.23.25 | - |
Debaryomyces hansenii |
3.4.24.37 | native enzyme 2560fold by fractionation with protamine sulfate, anion exchange chromatography on a weak followed by a strong anion exchange resin, and gel filtration | Debaryomyces hansenii |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.23.25 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | - |
Debaryomyces hansenii | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? | |
3.4.23.25 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | - |
Debaryomyces hansenii CECT 12487 | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? | |
3.4.23.25 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | - |
Debaryomyces hansenii CECT12487 | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? | |
3.4.24.37 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | - |
Debaryomyces hansenii | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? | |
3.4.24.37 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | - |
Debaryomyces hansenii CECT 12487 | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? | |
3.4.24.37 | N-succinyl-Leu-Tyr-7-amido-4-methylcoumarin + H2O | - |
Debaryomyces hansenii CECT12487 | N-succinyl-Leu-Tyr + 7-amino-4-methylcoumarin | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.23.25 | monomer | 1 * 42000, SDS-PAGE, native mass by gel filtration | Debaryomyces hansenii |
3.4.24.37 | monomer | 1 * 65000, SDS-PAGE | Debaryomyces hansenii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.23.25 | PRA | - |
Debaryomyces hansenii |
3.4.23.25 | Protease A | aspartic protease | Debaryomyces hansenii |
3.4.24.37 | PrD | - |
Debaryomyces hansenii |
3.4.24.37 | protease D | - |
Debaryomyces hansenii |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.24.37 | 37 | - |
assay at | Debaryomyces hansenii |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.4.23.25 | 5 | 6 | - |
Debaryomyces hansenii |
3.4.24.37 | 7 | 8 | - |
Debaryomyces hansenii |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.4.23.25 | 4 | 8 | very low activity at other pH | Debaryomyces hansenii |