3.4.24.32: beta-Lytic metalloendopeptidase
This is an abbreviated version!
For detailed information about beta-Lytic metalloendopeptidase, go to the full flat file.
Word Map on EC 3.4.24.32
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3.4.24.32
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3.4.24.4
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thermolysin
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achromobacter
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lyticus
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bacteriolytic
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thermoproteolyticus
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biotechnology
- 3.4.24.32
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3.4.24.4
- thermolysin
- achromobacter
- lyticus
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bacteriolytic
- thermoproteolyticus
- biotechnology
Reaction
Cleavage of N-acetylmuramoyl-/-Ala, and of the insulin B chain at Gly23-/-Phe > Val18-/-Cya =
Synonyms
Achromopeptidase component, beta-lytic metalloproteinase, beta-Lytic protease, blp, EC 3.4.24.4, EC 3.4.99.13, Myxobacter AL-1 proteinase I, Myxobacter beta-lytic proteinase, Myxobacter495 beta-lytic proteinase, Myxobacterium sorangium beta-lytic proteinase, Proteinase, beta lytic metallo-, Proteinase, Myxobacterium sorangium beta-lytic
ECTree
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Substrates Products
Substrates Products on EC 3.4.24.32 - beta-Lytic metalloendopeptidase
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REACTION DIAGRAM
L-pyroglutamyl-HWSYGLRPG-NH2 + H2O
L-pyroglutamyl-HWSYG + LRPG-NH2
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L-pyroglutamyl-QRLGNQWAVGHLM-NH2 + H2O
L-pyroglutamyl-QRLG + NQWAVGHLM-NH2
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L-pyroglutamyl-VPQWAVGHFM-NH2 + H2O
L-pyroglutamyl-VPQWAVG + HFM-NH2
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Hydrolyzed bacterial cell walls
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cleaves specific peptide bonds within the cell wall peptidoglycan network
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Lysobacter enzymogenes enzyme: Arthrobacter globiformis cells
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Micrococcus lysodeikticus cells
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Arthrobacter crystallopoietes cells walls
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Bacterial cell walls + H2O
Hydrolyzed bacterial cell walls
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Arthrobacter crystallopoietes cells walls
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Hydrolyzed insulin B-chain
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does not act on A-chain of oxidized insulin, it cleaves the B-chain readily at Gly23-Phe24 and more slowly at Val18-Cys19-SO3H
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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hydrolysis of Ala-Leu bond
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Insulin B-chain + H2O
Hydrolyzed insulin B-chain
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hydrolysis of Ala-Leu bond
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the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms
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additional information
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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
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additional information
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the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms
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additional information
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affinity towards peptide bonds formed by at least one hydrophobic amino acid in a structure at least as large as a tetrapeptide
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additional information
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affinity towards peptide bonds formed by at least one hydrophobic amino acid in a structure at least as large as a tetrapeptide
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