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Literature summary for 3.4.24.28 extracted from
- Specificity of megateriopeptidase: an amino-endopeptidase with hydrophobic characteristics (1969), Eur. J. Biochem., 9, 456-462.
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Priestia megaterium | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Priestia megaterium | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | specificity overview: peptide bonds in which leucine is involved by its amino group are rapidly split, then those of phenylalanine and lastly those of other hydrophobic residues. The residue involved in the bond by the carboxyl group may have a stimulating effect | Priestia megaterium | ? | - |
? |  |
| additional information | not: benzoyl-Gly-Phe, benzoyl-Gly-Leu (carboxypeptidase A substrates), benzoyl-Gly-Arg, benzoyl-Gly-Lys (carboxypeptidase B substrates), amides (Gly-NH2, Ser-NH2, His-NH2, Arg-NH2, Met-NH2, Leu-NH2, Phe-NH2, Tyr-NH2, Trp-NH2), benzoyl-Arg ethyl ester, tosyl-Arg methyl ester, benzoyl-Tyr ethyl ester | Priestia megaterium | ? | - |
? | |
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Release 2023.1 (January 2023)
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