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Literature summary for 3.4.24.75 extracted from

  • Surovtsev, V.I.; Borzenkov, V.M.; Fedorov, T.V.; Smotrov, O.I.
    Ionogenic groups in the active site of lysostaphin. Kinetic and thermodynamic data compared with x-ray crystallographic data (2007), Biochemistry (Moscow), 72, 989-993.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and thermodynamics Staphylococcus simulans

Organism

Organism UniProt Comment Textmining
Staphylococcus simulans
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biovar staphylolyticus, strain GNTs PM No. 1030
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Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of the -Gly-/-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans a two-stage reaction controlled by two ionogenic groups of the active site, the active site of lysostaphin contains glutamic acid and lysine Staphylococcus simulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information pentaglycine bridges in peptidoglycan of Staphylococci as a substrate Staphylococcus simulans ?
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?

Synonyms

Synonyms Comment Organism
More lysostaphin-type enzymes belong to so-called LAS, i.e. Lysostaphin, D-Ala-D-Ala carboxypeptidase, Sonic hedgehog enzyme, enzymes Staphylococcus simulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Staphylococcus simulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
the pH value near a negatively charged cell is supposed to be strongly shifted to acidity as compared to the pH of the solution volume. This shifts the enzyme pH dependence curve in solution to alkalinity, overview Staphylococcus simulans

pH Range

pH Minimum pH Maximum Comment Organism
4.5 10.3
-
Staphylococcus simulans