Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Cloned

Cloned on EC 3.4.21.12 - alpha-lytic endopeptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression of recombinant enzymes in Escherichia coli
-
mutant enzyme precursor with a pro region lacking its last three amino acids: the turnover number of folding of the mutant enzyme is 1000fold lower that for the folding of the wild type enzyme. Mutant enzyme precursor with a pro region lacking its last three amino acids and two additional mutations, R102H and G134S: turnover number of folding of the mutant enzyme is 2fold higher than that of the wild-type enzyme
-