Summary for peptidase A01.018: saccharopepsin

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Inhibitors Pharma

 

Names
MEROPS Namesaccharopepsin
Other namesallergen Rhi o 1 (Rhizopus oryzae), aspartic proteinase (Neurospora), Neurospora aspartic proteinase, neurosporapepsin, PEP2 g.p. (Aspergillus fumigatus), pep-4 g.p. (Neurospora crassa), PEP4 g.p. (Saccharomyces cerevisiae), peptidase E (Aspergillus fumigatus), Saccharomyces cerevisiae aspartic proteinase, yeast proteinase A, yscA g.p. (Saccharomyces cerevisiae)
Domain architecture
MEROPS Classification
Classification Clan AA >> Subclan (none) >> Family A1 >> Subfamily A >> A01.018
Holotypesaccharopepsin (Saccharomyces cerevisiae), Uniprot accession P07267 (peptidase unit: 78-405), MERNUM MER0000941
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeAspartic
PeplistIncluded in the Peplist with identifier PL00016
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.25
EnzymologyBRENDA database
Proteolytic eventsCutDB database (3 cleavages)
PhysiologyFunctions in the processing of procerevisin to the active endopeptidase (S08.052) in the vacuolar proteolytic system of Saccharomyces (Van den Hazel et al., 1996).
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/-Scissile bond-/-/-/- (based on 14 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 0 1 1 0 1 1 0 1
Pro 2 0 0 0 0 0 1 1
Ala 1 2 2 0 0 0 0 0
Val 3 1 2 0 1 1 1 0
Leu 1 0 2 3 2 3 2 0
Ile 0 1 0 0 0 1 0 0
Met 0 0 0 0 1 1 1 0
Phe 3 2 1 4 2 1 0 0
Tyr 0 1 0 1 3 2 0 0
Trp 0 0 1 1 1 0 0 0
Ser 0 0 1 0 0 0 0 1
Thr 0 0 1 1 0 1 2 2
Cys 0 0 0 0 0 0 0 0
Asn 0 0 0 1 0 1 1 1
Gln 0 1 1 1 0 0 0 0
Asp 1 0 0 0 0 0 2 2
Glu 2 2 1 1 1 0 0 0
Lys 0 0 1 1 1 0 1 1
Arg 1 2 0 0 0 2 0 0
His 0 1 0 0 0 0 1 0