Summary for peptidase M35.001: penicillolysin

Summary Alignment Sequences Sequence features Distribution Literature Substrates

 

Names
MEROPS Namepenicillolysin
Other namesfungal acid metalloendopeptidase
Domain architecture
MEROPS Classification
Classification Clan MA >> Subclan MA(D) >> Family M35 >> Subfamily (none) >> M35.001
Holotypepenicillolysin (Penicillium citrinum), Uniprot accession P47189 (peptidase unit: 174-351), MERNUM MER0001399
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
NC-IUBMBNot yet included in IUBMB recommendations.
Proteolytic eventsCutDB database (9 cleavages)
PhysiologyImportant in fungal nutrition.
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/-Scissile bondlr/-/-/- (based on 20 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 2 2 2 1 3 0 2 1
Pro 1 2 1 4 0 2 2 3
Ala 0 1 0 1 1 0 0 0
Val 0 1 1 0 0 1 0 2
Leu 1 1 3 2 5 4 1 2
Ile 0 1 0 0 0 1 0 1
Met 1 0 0 0 0 2 1 0
Phe 0 3 3 4 0 0 3 1
Tyr 1 0 0 3 1 2 3 2
Trp 0 1 0 2 0 1 0 0
Ser 0 0 2 0 3 0 0 0
Thr 0 0 0 0 0 0 0 0
Cys 0 0 0 0 0 0 0 0
Asn 1 1 0 0 0 0 1 0
Gln 2 1 0 0 1 1 0 0
Asp 0 0 0 0 0 0 0 0
Glu 2 1 1 1 0 1 1 0
Lys 0 1 2 0 1 2 2 2
Arg 2 0 2 2 5 3 2 1
His 3 0 2 0 0 0 0 1