3.4.21.12: alpha-lytic endopeptidase
This is an abbreviated version!
For detailed information about alpha-lytic endopeptidase, go to the full flat file.
Reaction
preferential cleavage: Ala-/-, Val-/- in bacterial cell walls, elastin and other proteins =
Synonyms
ALP, Alpha-lytic endopeptidase, alpha-lytic protease, alpha-lytic proteinase, alphaLP, bacteriolytic protease L5, Mycobacterium sorangium alpha-lytic proteinase, Myxobacter 495 alpha-lytic proteinase, Myxobacter alpha-lytic proteinase, protein L5, proteinase, Mycobacterium sorangium alpha-lytic, proteinase, Myxobacter alpha-lytic
ECTree
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Substrates Products
Substrates Products on EC 3.4.21.12 - alpha-lytic endopeptidase
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REACTION DIAGRAM
Abz-Ala-Ala-Phe-4-nitroanilide + H2O
Abz-Ala-Ala-Phe + 4-nitroaniline
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
Staphylococcus aureus peptidoglycan + H2O
?
the enzyme possesses a Gly-Gly endopeptidase activity with respect to staphylococcal peptidoglycan and an amidase that manifests an N-acetylmuramoyl-L-Ala amidase activity with respect to this substrate
-
-
?
succinyl-Ala-Ala-Pro-Ala-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Ala + 4-nitroaniline
-
high activity with wild-type enzyme and mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Leu + 4-nitroaniline
-
weak activity with wild-type enzyme, high activity with mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
weak activity with wild-type enzyme, high activity with mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-Val-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Val + 4-nitroaniline
-
high activity with wild-type enzyme and mutant enzyme M190A
-
?
succinyl-Ala-Ala-Pro-X-p-nitroanilide + H2O
?
-
X: Gly, Thr, Val, Leu, Ile, Met, Phe
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala 4-nitroanilide + H2O
N-succinyl-L-Ala-L-Ala-L-Ala + 4-nitroaniline
-
-
-
-
?
?
-
-
oligopeptides on the carbonyl side of amino acids with short neutral aliphatic side-chains
-
-
?
additional information
?
-
-
carbonyl end of small residues as Val, Ser, Val
-
-
?
additional information
?
-
-
preferential cleavage of bonds adjacent to L-alanine
-
-
?
additional information
?
-
-
carbonyl end of small residues as Val, Ser, Val
-
-
?
additional information
?
-
-
preferential cleavage of bonds adjacent to L-alanine
-
-
?