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Literature summary for 3.4.21.12 extracted from

  • Mace, J.E.; Agard, D.A.
    Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity (1995), J. Mol. Biol., 254, 720-736.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant enzymes in Escherichia coli Lysobacter enzymogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Lysobacter enzymogenes

Protein Variants

Protein Variants Comment Organism
G216A active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216D no active enzyme Lysobacter enzymogenes
G216F active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216G active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216H active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216I active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216K no active enzyme Lysobacter enzymogenes
G216L active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216N no active enzyme Lysobacter enzymogenes
G216P no active enzyme Lysobacter enzymogenes
G216Q active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216R no active enzyme Lysobacter enzymogenes
G216S active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216T active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216V active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216W active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes
G216Y active enzyme, but production levels for the mutants with larger substitutions do decrease significantly Lysobacter enzymogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Lysobacter enzymogenes

Organism

Organism UniProt Comment Textmining
Lysobacter enzymogenes
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
succinyl-Ala-Ala-Pro-X-p-nitroanilide + H2O X: Gly, Thr, Val, Leu, Ile, Met, Phe Lysobacter enzymogenes ?
-
?