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Literature summary extracted from
- Beta-lytic metalloendopeptidase (2004), Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press, 1, 998-1000.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.24.32 | additional information | ability to lyse Arthrobacter globiformis, Micrococcus luteus and Staphylococcus aureus cells, inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent | Lysobacter enzymogenes |
| 3.4.24.32 | additional information | ability to lyse Micrococcus luteus and Staphylococcus aureus cells | Achromobacter lyticus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.24.32 | - |
Lysobacter enzymogenes |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.32 | 1,10-phenanthroline | - |
Lysobacter enzymogenes |  |
| 3.4.24.32 | additional information | insensitive to DFP | Lysobacter enzymogenes |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.24.32 | Zn2+ | required for activity | Achromobacter lyticus | |
| 3.4.24.32 | Zn2+ | required for activity | Lysobacter enzymogenes | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.32 | 19100 | - |
- |
Lysobacter enzymogenes |
| 3.4.24.32 | 19300 | - |
- |
Achromobacter lyticus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.24.32 | Achromobacter lyticus | - |
- |
- |
| 3.4.24.32 | Lysobacter enzymogenes | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.24.32 | - |
Achromobacter lyticus |
| 3.4.24.32 | - |
Lysobacter enzymogenes |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.24.32 | casein + H2O | - |
Lysobacter enzymogenes | ? | - |
? | |
| 3.4.24.32 | elastin-orcein + H2O | - |
Lysobacter enzymogenes | ? | - |
? | |
| 3.4.24.32 | furylacryloyl-Gly-Leu-NH2 + H2O | - |
Lysobacter enzymogenes | ? | - |
? | |
| 3.4.24.32 | Insulin B-chain + H2O | - |
Lysobacter enzymogenes | ? | - |
? | |
| 3.4.24.32 | additional information | no cleavage of Z-Gly-Phe | Lysobacter enzymogenes | ? | - |
? | |
| 3.4.24.32 | additional information | the enzyme only cleaves Gly-X bonds and favors hydrophobic or apolar residues to either side, it does not hydrolyze bonds with charged amino acids or proline adjacent, cleaves D-Ala-Gly and D-Ala-Ala bonds in the linkage between peptide subunit and the interpeptide bridge and also the Gly-Gly bond in the Staphylococcus aureus interpeptide bridge | Achromobacter lyticus | ? | - |
? | |
| 3.4.24.32 | peptidoglycan + H2O | - |
Achromobacter lyticus | ? | - |
? | |
| 3.4.24.32 | peptidoglycan + H2O | - |
Lysobacter enzymogenes | ? | - |
? | |
| 3.4.24.32 | Z-Gly-Phe-NH2 + H2O | - |
Lysobacter enzymogenes | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.24.32 | beta-Lytic protease | - |
Achromobacter lyticus |
| 3.4.24.32 | beta-Lytic protease | - |
Lysobacter enzymogenes |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.24.32 | 6.5 | - |
for FA-Gly-Leu-NH2 hydrolysis | Lysobacter enzymogenes |
| 3.4.24.32 | 9 | - |
for bacteriolysis | Lysobacter enzymogenes |
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Release 2023.1 (January 2023)
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