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(MCA)Glu-Val-Lys-Met-Asp-Ala-Glu-Phe-Lys(DNP) + H2O
(MCA)Glu-Val-Lys-Met + Asp-Ala-Glu-Phe-Lys(DNP)
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synthetic peptide substrate based on the beta-secretase cleavage site of wild-type APP
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amyloid precursor protein + H2O
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the enzyme cleaves amyloid precursor protein within the Abeta domain, particularly at the zeta-site (Phe20) to produce fragment C80 and prevents Abeta generation
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
amyloid-alpha pecursor protein + H2O
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amyloid-beta precursor protein + H2O
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beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
collectrin + H2O
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delta and notch-like epidermal growth factor-related receptor + H2O
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DELTA322-IL-1R2 + H2O
fragments of DELTA322-IL-1R2
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truncated protein cotransfected with the enzyme in HEK 293
cleavage in the same manner as for the full length protein with cleavage between Phe329 and Gln330
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fibroblast growth factor receptor 1 + H2O
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gamma-secretase cleavage site of notch + H2O
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NCH-gamma
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IL-1R2 + H2O
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synthetic peptide from Val322 to Ser341
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IL-1R2 + H2O
fragments of IL-1R2
insulin B chain + H2O
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only pro-BACE2-T1
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kinetensin + H2O
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Mastoparan + H2O
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neuropetide + H2O
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Met-Lys-Arg-Ser-Arg-Gly-Pro-Ser-Pro-Arg-Arg
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pigment cell-specific melanocyte protein + H2O
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BACE2 processes pigment cell-specific melanocyte protein to generate functional amyloids. BACE2 cleaves the integral membrane form of pigment cell-specific melanocyte protein within the juxtamembrane domain, releasing the luminal domain into endosomal precursors for the formation of amyloid fibrils and downstream melanosome morphogenesis
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plexin domain containing 2 + H2O
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preproenkephalin fragment 128-140 + H2O
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preproenkephalin fragment 129-138 + H2O
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ENK-1
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rhodamine-EVNLDAEFK-quencher + H2O
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FRET-substrate
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Swedish amyloid-beta pecursor protein + H2O
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Tmem27 + H2O
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proliferative plasma membrane protein
BACE2 inactivates Tmem27 by cleavage to release a 25000 Da N-terminal part and a 22000 Da C-terminal fragment
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vascular cell adhesion molecule 1 + H2O
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proinflammatory tumor necrosis factor induces a drastic increase in enzyme-mediated shedding of vascular cell adhesion molecule 1 in cerebrospinal fluid
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additional information
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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able to cleave the beta-site but preferential cleavage of amyloid precursor protein (APP) downstream of the alpha-site of A-beta (after Phe19, theta-site), not involved in the Alzheimers disease pathogenesis in Down syndrome patients, able to reduce A-beta formation when expressed in primary neurons expressing the Swedish mutant of APP
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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can cleave the amyloid precursor protein (APP) at the N terminal Asp-1 position of A-beta, preferential cleavage within the A-beta region at Phe19 or Phe20, enzyme function is not consistent with a requirement and function of BACE1 as a beta-secretase in the brain, may act antagonistically to BACE1
soluble ectodomain (sAPPb),and a membrane-bound APP C-terminal fragment of 99 amino acids
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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cleavage at the beta site of amyloid precursor protein but preferably between Phe690 and Phe691 or Phe691 and Ala692
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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cleavage at the beta-site but more effectively at a different site within A-beta, non-amyloidogenic function suggested
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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cleavage after Phe19
resulting N-terminal sequence is FAEDVGSN
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amyloid precursor protein + H2O
fragments of amyloid precursor protein
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amyloid-beta precursor protein + H2O
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amyloid-beta precursor protein + H2O
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amyloid-beta precursor protein + H2O
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amyloid-beta precursor protein + H2O
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amyloid-beta precursor protein + H2O
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results in increase of beta-secretase-derived soluble amyloid precursor protein and the corresponding carboxy-terminal fragment
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amyloid-beta precursor protein + H2O
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cleaves after the Phe19 and Phe20
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amyloid-beta precursor protein + H2O
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cleaves in the middle of the amyloid-beta protein domain between Phe19 and Phe20, resulting in increased secretion of amyloid precursor proteins-alpha- and p3-like products
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amyloid-beta precursor protein + H2O
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results in 40-42 residue amyloid-beta peptide
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amyloid-beta precursor protein + H2O
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beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
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beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
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beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
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cleavage at KLVF-/-FAED and at LVFF-/-AEDV, and with low activity at EVKM-/-DAEF
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beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
cleavage at the beta-site
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IL-1R2 + H2O
fragments of IL-1R2
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cleavage produces fragments which are almost identical to those produced by alpha-sectretase, enzyme might act in an alternative alpha-sectretase like cleavage
cleavage between Phe329 and Gln330
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IL-1R2 + H2O
fragments of IL-1R2
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intact recombinant protein with a mass of 2219.7 Da
fragments with masses of 916.7 Da and 1321 Da indicating a cleavage between Phe329 and Gln330
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Swedish amyloid-beta pecursor protein + H2O
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Swedish amyloid-beta pecursor protein + H2O
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additional information
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BACE2 cleaves at the beta site and more efficiently at a different site within amyloid-beta precursor protein
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additional information
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the enzyme is involved in Alzheimer's disease
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additional information
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the enzyme might be involved in Alzheimer's disease
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additional information
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the enzyme might be involved in Alzheimer's disease
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additional information
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the enzyme might be involved in Alzheimer's disease
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additional information
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the enzyme might be involved in early onset of dementia in patients with Down syndrome, and is highly expressed in breast cancers, the enzyme may also be involved in muscle functions
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additional information
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autoactivation in an acidic solution with cleavage of the own propeptide within the sequence Gly-leu-Ala-Leu--/-Ala-Leu-Glu-Pro
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additional information
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P-selctin, TNF-alpha and CD14 are not cleaved
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additional information
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BACE-2 exhibits secretase activity with cleavage in the middle of the amyloid peptide domain at amino acids 19 and 20 generating a carboxy-terminal fragment of 79 residues, and does not contribute to the process of amyloid peptide generation, BACE-2 can cleave at the beta-site, but consistent with its different substrate specificity, does not cleave a preferred peptide-based BACE-1 substrate
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additional information
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enzyme additionally degrades amyloid beta-protein, with a catalytic efficiency similar to insulin-degrading enzyme IDE, EC 3.4.23.56
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additional information
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screen for substrate proteins in pancreatic beta cells by proteomic approach reveals non-redundant roles of BACE1 and BACE2 in ectodomain shedding, with BACE1 regulating a broader and BACE2 a more distinct set of beta-cell-enriched substrates including two proteins of the seizure 6 protein family, SEZ6L and SEZ6L2
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