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Literature summary for 3.4.21.12 extracted from

  • Ota, N.; Agard, D.A.
    Enzyme specificity under dynamic control II: Principal component analysis of alpha-lytic protease using global and local solvent boundary conditions (2001), Protein Sci., 10, 1403-1414.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.12

Protein Variants

Protein Variants Comment Organism
M190A mutation broadens specificity while maintaining or increasing catalytic activity Lysobacter enzymogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Lysobacter enzymogenes
-
-

Organism

Organism UniProt Comment Textmining
Lysobacter enzymogenes
-
-
-

Reaction

Reaction Comment Organism Reaction ID
preferential cleavage: Ala-/-, Val-/- in bacterial cell walls, elastin and other proteins the specificity mechanism of the enzyme is influenced by dynamic motion around the S1 binding pocket in addition to the static structural characteristics Lysobacter enzymogenes
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide + H2O high activity with wild-type enzyme and mutant enzyme M190A Lysobacter enzymogenes succinyl-Ala-Ala-Pro-Ala + 4-nitroaniline
-
 ?
succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O weak activity with wild-type enzyme, high activity with mutant enzyme M190A Lysobacter enzymogenes succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
 ?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O weak activity with wild-type enzyme, high activity with mutant enzyme M190A Lysobacter enzymogenes succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
 ?
succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O high activity with wild-type enzyme and mutant enzyme M190A Lysobacter enzymogenes succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
 ?