Summary for peptidase M23.001: beta-lytic metallopeptidase

Summary Alignment Sequences Sequence features Distribution Literature Substrates Inhibitors

 

Names
MEROPS Namebeta-lytic metallopeptidase
Other namesachromopeptidase component
Domain architecture
MEROPS Classification
Classification Clan MO >> Subclan (none) >> Family M23 >> Subfamily A >> M23.001
Holotypebeta-lytic metallopeptidase (Achromobacter lyticus), Uniprot accession P27458 (peptidase unit: 196-374), MERNUM MER0001281
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00233
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.24 (Metalloendopeptidases) >> Peptidase 3.4.24.32
EnzymologyBRENDA database
PhysiologyLysis of other organisms for bacterial nutrition.
Pharmaceutical relevanceUse as antimicrobial agent has been considered.
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/ayf/-/GScissile bondhl/fm/m/- (based on 15 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 1 0 2 13 1 1 0 0
Pro 0 0 0 0 0 0 0 0
Ala 0 5 1 0 0 1 2 0
Val 0 0 3 1 0 0 0 0
Leu 1 0 1 0 4 1 0 0
Ile 0 0 2 0 0 0 0 0
Met 0 0 2 0 0 4 4 0
Phe 0 2 0 0 2 4 0 1
Tyr 0 3 0 0 0 0 1 0
Trp 2 1 0 0 2 1 0 0
Ser 0 0 0 0 0 0 1 1
Thr 0 0 1 0 0 0 0 2
Cys 0 0 0 0 0 0 0 0
Asn 0 0 0 1 1 1 0 0
Gln 0 0 0 0 0 0 0 0
Asp 1 0 0 0 0 0 2 0
Glu 0 1 0 0 0 0 1 0
Lys 1 0 0 0 0 0 0 0
Arg 0 0 1 0 0 0 0 1
His 0 0 0 0 4 0 0 0