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
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General Stability on EC 3.4.21.12 - alpha-lytic endopeptidase
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities
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kinetic stability impaired by the large, cooperative unfolding barrier plays a critical role in extending the lifetime of the protease in its harsh environment
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
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Pro N-domain both provides direct interactions with alpha-lytic protease that stabilize the folding transition state and confers stability to the Pro C-domain
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