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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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.12 alpha-lytic endopeptidase

Crystallization

Crystallization on EC 3.4.21.12 - alpha-lytic endopeptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure solved at 0.83 A resolution at pH 8
subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis
hanging drop vapor diffusion method, using 2.7 M sodium formate and 0.01 M PIPES, at pH 7.0