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Literature summary extracted from

  • Kessler, E.
    beta-Lytic endopeptidases (1995), Methods Enzymol., 248, 740-756.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.32 Lysobacter enzymogenes Lysobacter enzymogenes

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.32 1,10-phenanthroline
-
 Lysobacter enzymogenes
3.4.24.32 additional information diisopropylfluorophosphate Lysobacter enzymogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.32 Zinc Lysobacter enzymogenes enzyme contains a zinc atom Lysobacter enzymogenes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.32 19100
-
 Lysobacter enzymogenes, calculated from amino acid sequence Lysobacter enzymogenes
3.4.24.32 22000
-
 x * 22000 Achromobacter lyticus, SDS-PAGE Achromobacter lyticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.32 additional information Achromobacter lyticus the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms ?
-
 ?
3.4.24.32 additional information Lysobacter enzymogenes the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms ?
-
 ?

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 3-(2-Furylacryloyl)-Gly-Leu amide + H2O
-
 Lysobacter enzymogenes ?
-
 ?
3.4.24.32 Bacterial cell walls + H2O cleaves specific peptide bonds within the cell wall peptidoglycan network Lysobacter enzymogenes Hydrolyzed bacterial cell walls
-
 ?
3.4.24.32 Bacterial cell walls + H2O Lysobacter enzymogenes enzyme: Arthrobacter globiformis cells Lysobacter enzymogenes Hydrolyzed bacterial cell walls
-
 ?
3.4.24.32 Bacterial cell walls + H2O Micrococcus lysodeikticus cells Lysobacter enzymogenes Hydrolyzed bacterial cell walls
-
 ?
3.4.24.32 Benzyloxycarbonyl-Gly-Phe amide + H2O
-
 Lysobacter enzymogenes ?
-
 ?
3.4.24.32 casein + H2O limited activity Lysobacter enzymogenes hydrolyzed casein
-
 ?
3.4.24.32 Elastin-orcein + H2O
-
 Lysobacter enzymogenes Hydrolyzed elastin-orcein
-
 ?
3.4.24.32 Insulin B-chain + H2O 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 Lysobacter enzymogenes Hydrolyzed insulin B-chain
-
 ?
3.4.24.32 additional information the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms Achromobacter lyticus ?
-
 ?
3.4.24.32 additional information the primary biological role is the defense against bacteria in the environment, in particular against species of Staphylococcus or closely related organisms Lysobacter enzymogenes ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.32 ? x * 22000 Achromobacter lyticus, SDS-PAGE Achromobacter lyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.32 6.5
-
 3-(2-furylacryloyl)-Gly-Leu-amide, Lysobacter enzymogenes Lysobacter enzymogenes
3.4.24.32 8.5 9 bacteriolysis, Lysobacter enzymogenes Lysobacter enzymogenes