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Literature summary for 3.4.21.12 extracted from

  • Haddad, K.C.; Sudmeier, J.L.; Bachovchin, D.A.; Bachovchin, W.W.
    alpha-Lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities (2005), Proc. Natl. Acad. Sci. USA, 102, 1006-1011.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities Lysobacter enzymogenes
lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity Lysobacter enzymogenes

Inhibitors

Inhibitors Comment Organism Structure
additional information lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity Lysobacter enzymogenes

Organism

Organism UniProt Comment Textmining
Lysobacter enzymogenes
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Ala-Pro-Ala-4-nitroanilide + H2O
-
Lysobacter enzymogenes ?
-
?

Synonyms

Synonyms Comment Organism
alpha-lytic protease
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Lysobacter enzymogenes