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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results (Inhibitors
Inhibitors on EC 3.4.21.12 - alpha-lytic endopeptidase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
guanidine hydrochloride
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1% residual activity in the presence of 4 mM guanidine hydrochloride
methoxysuccinyl-Ala-Ala-Pro-L-boroPhe
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the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates close to tetrahedral boron coordination in the active site of the enzyme/inhibitor complex
methoxysuccinyl-Ala-Ala-Pro-L-boroVal
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the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates tetrahedral boron coordination in the active site of the enzyme/inhibitor complex
N-terminal 166 amino acid Pro region of alpha-lytic protease
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dual role of folding and inhibition
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Turkey ovomucoid third domain
OMTKY3, very weak inhibitor, different mutations in the inhibitory protein are found to affect the inhibitory effect
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Turkey ovomucoid third domain
Turkey Ovomucoid Third Domain (OMTKY3) inhibits the enzyme much more weakly (by about 1000000times) than eglin C. A variant of OMTKY3 with five mutations K13A/P14E/L18A/R21T/N36D inhibits 10000times more strongly than the wild type inhibitor
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additional information
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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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