Summary for peptidase M12.145: atrolysin E

Summary Alignment Sequences Sequence features Distribution Literature Substrates Inhibitors

 

Names
MEROPS Nameatrolysin E
Other namesatrolysin E/D, barnettlysin-I (Bothrops barnetti), hemorrhagic toxin e (Crotalus atrox), metalloendopeptidase e (Crotalus atrox)
Domain architecture
MEROPS Classification
Classification Clan MA >> Subclan MA(M) >> Family M12 >> Subfamily B >> M12.145
Holotypeatrolysin E (Crotalus atrox), Uniprot accession P34182 (peptidase unit: 189-389), MERNUM MER0001137
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00186
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.24 (Metalloendopeptidases) >> Peptidase 3.4.24.44
EnzymologyBRENDA database
Proteolytic eventsCutDB database (9 cleavages)
PhysiologyLikely role in snake venom toxicity. Hemorrhagic.
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/agScissile bondL/gv/a/- (based on 19 cleavages)
weblogo
Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 2 3 2 4 0 5 3 2
Pro 1 0 1 0 0 0 0 0
Ala 0 2 3 8 1 2 4 1
Val 1 2 4 1 0 5 1 1
Leu 2 0 1 1 11 2 2 1
Ile 0 0 0 0 0 0 0 0
Met 1 0 0 0 1 0 0 0
Phe 0 1 0 0 1 1 0 0
Tyr 0 0 0 1 0 1 1 1
Trp 0 0 0 0 0 0 0 0
Ser 0 1 1 1 1 0 0 2
Thr 0 0 0 0 0 0 0 1
Cys 0 0 0 0 0 0 0 0
Asn 0 1 0 1 0 0 0 0
Gln 1 0 2 0 2 0 0 0
Asp 0 0 1 0 0 0 0 0
Glu 2 2 1 0 0 0 1 2
Lys 0 0 0 0 0 0 1 0
Arg 0 0 2 0 0 0 2 0
His 0 0 0 2 2 1 0 0