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, Mycobacterium sorangium alpha-lytic proteinase, Myxobacter 495 alpha-lytic proteinase, Myxobacter alpha-lytic proteinase, proteinase, Mycobacterium sorangium alpha-lytic, proteinase, Myxobacter alpha-lytic

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.12 alpha-lytic endopeptidase

Engineering

Engineering on EC 3.4.21.12 - alpha-lytic endopeptidase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G216A
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216D
-
no active enzyme
G216F
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216G
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216H
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216I
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216K
-
no active enzyme
G216L
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216N
-
no active enzyme
G216P
-
no active enzyme
G216Q
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216R
-
no active enzyme
G216S
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216T
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216V
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216W
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216Y
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
additional information
-
Pro region N-domain mutants: disruption of the hydrogen bonding potentials of Y26 and E30 primarily alters Pro binding to the folding transition state as compared to binding in the initial and native state complexes