enzymatic reaction

Solubilized Clipsin degrades APP and both succinyl AAPF- & methoxy-succinyl AAPM-p-nitroanilides. The A4 peptide is said to contain NH2-terminal methionine.

Properties

GENERAL: catalytic reaction SPECIFIC: biochemical ligation sialylation active transport protein phosphorylation proteolytic cleavage template-directed reaction ENZYME: clipsin COMPARTMENT: tissue WITHIN: brain ORGANISM: Rattus (rat) STATE: active state MOTIF: S1 domain {1} SUBSTRATE: amyloid precursor protein COMPARTMENT: tissue WITHIN: brain ORGANISM: Rattus (rat) MOTIF: cysteine-rich region sulfotyrosine site MODIFICATION: sulfate Zn+2-binding site acidic region MOTIF: acidic residue (SEVERAL) binding site FOR-BINDING-OF: heparan sulfate binding site FOR-BINDING-OF: collagenase-4 MOTIF: O-glycosylation site N-glycosylation site (2) domain MOTIF: proteolytic site transmembrane domain {627-648} Thr phosphorylation site {T654} Ser phosphorylation site {S655} binding site FOR-BINDING-OF: Go protein NPXY motif NAME: NPXY motif FOR-BINDING-OF: amyloid beta A4 protein-binding family B member 1 MOTIF-SEQUENCE: Asn-Pro-Thr-Tyr PRECURSOR-FOR: A4 amyloid peptide COMPARTMENT: extracellular compartment INHIBITS: collagenase-4 PRODUCT: peptide QUALITIES: *SEQUENCE* :NH2_TERMINAL METHIONINE-RES COMPARTMENT: tissue WITHIN: brain ORGANISM: Rattus (rat) peptide QUALITIES: *SEQUENCE* :NH2_TERMINAL PHENYLALANINE-RES COMPARTMENT: tissue WITHIN: brain ORGANISM: Rattus (rat)

References

- Nelson RB, Siman R. Clipsin, a chymotrypsin-like protease in rat brain which is irreversibly inhibited by alpha-1-antichymotrypsin. J Biol Chem. 1990 Mar 5;265(7):3836-43. PMID: 2303481