Literature summary for 3.4.21.96 extracted from

Visser, S.; Robben, A.J.P.M.; Slangen, C.J.
Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine beta-casein (1991), Appl. Microbiol. Biotechnol., 35, 477-483.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell envelope	-	Lactococcus lactis	30313	-

Organism

Organism	UniProt	Comment	Textmining
Lactococcus lactis	-	subsp. cremoris strain AM1	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-Casein + H2O	PIII-type proteinase of subsp. cremoris AM1 preferentially cleaves 16 peptide bonds, the cleavage sites are primarily Gln-X or Glu-X, mostly a large hydrophobic residue is part of the cleavable position, a hydrophobic residue is frequently at position P2, sometimes also at P2', one or more side chains in P2-P3 or P2'-P3' are negetively charged	Lactococcus lactis	Fragments of beta-casein	-	?

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Release 2023.1 (January 2023)