Summary for peptidase M34.001: anthrax lethal factor

Summary Alignment Sequences Sequence features Distribution Structure Literature Substrates Inhibitors Pharma

 

Names
MEROPS Nameanthrax lethal factor
Other nameslethal toxin, anthrax, LeTx
Domain architecture
MEROPS Classification
Classification Clan MA >> Subclan MA(E) >> Family M34 >> Subfamily (none) >> M34.001
Holotypeanthrax lethal factor (Bacillus anthracis), Uniprot accession P15917 (peptidase unit: 585-809), MERNUM MER0001345
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeMetallo
PeplistIncluded in the Peplist with identifier PL00250
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.24 (Metalloendopeptidases) >> Peptidase 3.4.24.83
EnzymologyBRENDA database
Proteolytic eventsCutDB database (8 cleavages)
PhysiologyAnthrax virulence determinant that inactivates mitogen-activated protein kinase kinase, so killing infected macrophages (Ascenzi et al., 2002).
Pharmaceutical relevanceCytotoxic component of anthrax toxin. A urokinase-activated form is a potential antitumour agent (Liu et al., 2003).
Pathways KEGGNOD-like receptor signaling pathway
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage patternKp/-/Lt/pScissile bondily/pq/l/ne (based on 12 cleavages)
weblogo
Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 1 0 1 0 0 0 0
Pro 3 3 0 5 0 5 0 0
Ala 0 1 1 0 1 0 0 2
Val 0 2 0 0 0 0 0 0
Leu 0 0 7 0 3 1 6 0
Ile 0 0 0 0 5 0 0 1
Met 0 1 0 1 0 0 1 1
Phe 0 0 0 0 1 0 1 0
Tyr 0 0 1 0 2 0 0 0
Trp 0 1 0 0 0 0 0 0
Ser 1 0 0 0 0 1 1 0
Thr 0 2 3 0 0 1 1 1
Cys 0 0 0 0 0 0 1 0
Asn 0 0 0 0 0 1 0 4
Gln 0 0 0 1 0 3 0 0
Asp 0 1 0 0 0 0 0 0
Glu 0 0 0 0 0 0 0 3
Lys 7 0 0 2 0 0 1 0
Arg 0 0 0 2 0 0 0 0
His 1 0 0 0 0 0 0 0