ID   3.4.26.2
DE   scytalidoglutamic peptidase.
AN   scytalidocarboxylpeptidase-B.
AN   scytalidopepsin-B.
CA   Hydrolysis of proteins, with a strong preference for Phe or Tyr at
CA   position P1 and one of the smaller amino-acids at P1' in the sequence -
CA   P3 - P2 - P1 -|-P1'- P2'- P3'-. Cleaves the Tyr(26)-Thr(27) bond in the B
CA   chain of oxidized insulin, which is not cleaved by pepsin.
CC   -!- The enzyme, isolated from the fungus Scytalidium lignicola and found
CC       in several other fungi, has a low pH optimum, being most active at pH
CC       2 with casein as substrate.
CC   -!- It differs from the EC 3.4.23.1 and EC 3.4.23.2 in being insensitive
CC       to inhibition by pepstatin. It also differs from mammalian pepsins in
CC       showing a preference for a positively charged residue (Lys or Arg) at
CC       the P3 position.
CC   -!- In addition to the catalytic Glu residue, a Gln residue appears to
CC       play an important role in the hydrolytic mechanism.
CC   -!- A member of peptidase family G01, the "eqolisin" family of glutamic
CC       peptidases (G01.0001).
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