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.
Word Map on EC 3.4.21.12
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
3.4.21.12 alpha-lytic endopeptidaseAdvanced search results
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Engineering on EC 3.4.21.12 - alpha-lytic endopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G216A
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
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
G216L
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
G216Q
-
active enzyme, but production levels for the mutants with larger substitutions do decrease significantly
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
M190A
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
M190A
-
mutation broadens specificity while maintaining or increasing catalytic activity
