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Information on EC 3.4.23.45 - memapsin 1 and Organism(s) Homo sapiens and UniProt Accession Q9Y5Z0
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3.4.23.45 memapsin 1Specify your search results
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
Synonyms
bace2, beta-site app cleaving enzyme, bace-2, memapsin 1, beta-secretase 2, bace 2, beta site app cleaving enzyme, beta-site app-cleaving enzyme 2, protease asp1, aspartic protease bace2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspartic protease BACE2
-
-
-
-
BACE2
beta-secretase
beta-secretase 2
beta-site Alzheimer's amyloid precurser protein cleaving enzyme 2
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-
-
-
beta-site amyloid precursor protein cleaving enzyme 2
-
-
-
-
beta-site APP-cleaving enzyme 2
-
-
-
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down region aspartic protease
-
-
-
-
protease ASP1
-
-
-
-
theta-secretase
-
preferential cleavage of the amyloid precursor protein downstream of the alpha-site of A-beta
additional information
BACE2
-
-
-
-
BACE2
-
homologue to BACE1, which cleaves amyloid precursor protein at the beta site but preferably after Phe690 or Phe691
beta-secretase
-
-
-
-
beta-secretase 2
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
active site structure, substrate binding structure, tetrahedral transition state intermediate
-
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
cleavage at the beta-site but more effectively at a different site within A-beta
-
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
preferential cleavage of amyloid precursor protein downstream of the alpha-site of A-beta (after Phe19, theta-site), resulting N-terminal sequence of product is FAEDVGSN
-
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
preferential cleavage of the amyloid precursor protein between Phe690 and Phe691 or Phe691 and Ala692
-
broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-/-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein
preferential cleavage within the A-beta region at Phe19 or Phe20
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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cleavage of C-N-linkage
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-
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CAS REGISTRY NUMBER
COMMENTARY
447457-31-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
(MCA)Glu-Val-Lys-Met-Asp-Ala-Glu-Phe-Lys(DNP) + H2O
(MCA)Glu-Val-Lys-Met + Asp-Ala-Glu-Phe-Lys(DNP)
-
synthetic peptide substrate based on the beta-secretase cleavage site of wild-type APP
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
DELTA322-IL-1R2 + H2O
fragments of DELTA322-IL-1R2
-
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
-
?
amyloid-beta precursor protein + H2O
?
results in increase of beta-secretase-derived soluble amyloid precursor protein and the corresponding carboxy-terminal fragment
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
-
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
cleavage at the beta-site
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
-
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
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 AlzheimerĀs disease pathogenesis in Down syndrome patients, able to reduce A-beta formation when expressed in primary neurons expressing the Swedish mutant of APP
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
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
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
cleavage at the beta site of amyloid precursor protein but preferably between Phe690 and Phe691 or Phe691 and Ala692
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
cleavage at the beta-site but more effectively at a different site within A-beta, non-amyloidogenic function suggested
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
cleavage after Phe19
resulting N-terminal sequence is FAEDVGSN
-
?
amyloid-beta precursor protein + H2O
?
-
-
-
-
?
amyloid-beta precursor protein + H2O
?
-
cleaves after the Phe19 and Phe20
-
-
?
amyloid-beta precursor protein + H2O
?
-
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
-
-
?
amyloid-beta precursor protein + H2O
?
-
results in 40-42 residue amyloid-beta peptide
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
-
-
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
-
cleavage at KLVF-/-FAED and at LVFF-/-AEDV, and with low activity at EVKM-/-DAEF
-
-
?
IL-1R2 + H2O
fragments of IL-1R2
-
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
-
?
IL-1R2 + H2O
fragments of IL-1R2
-
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
-
?
additional information
?
-
the enzyme might be involved in Alzheimer's disease
-
-
?
additional information
?
-
-
the enzyme might be involved in Alzheimer's disease
-
-
?
additional information
?
-
enzyme additionally degrades amyloid beta-protein, with a catalytic efficiency similar to insulin-degrading enzyme IDE, EC 3.4.23.56
-
-
?
additional information
?
-
-
BACE2 cleaves at the beta site and more efficiently at a different site within amyloid-beta precursor protein
-
-
?
additional information
?
-
-
the enzyme is involved in Alzheimer's disease
-
-
?
additional information
?
-
-
the enzyme might be involved in Alzheimer's disease
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
autoactivation in an acidic solution with cleavage of the own propeptide within the sequence Gly-leu-Ala-Leu--/-Ala-Leu-Glu-Pro
-
-
?
additional information
?
-
-
P-selctin, TNF-alpha and CD14 are not cleaved
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
-
-
-
?
amyloid-beta precursor protein + H2O
?
-
-
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
IL-1R2 + H2O
fragments of IL-1R2
-
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
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
-
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
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 AlzheimerĀs disease pathogenesis in Down syndrome patients, able to reduce A-beta formation when expressed in primary neurons expressing the Swedish mutant of APP
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
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
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
cleavage at the beta site of amyloid precursor protein but preferably between Phe690 and Phe691 or Phe691 and Ala692
-
-
?
amyloid precursor protein + H2O
fragments of amyloid precursor protein
-
cleavage at the beta-site but more effectively at a different site within A-beta, non-amyloidogenic function suggested
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
-
-
-
-
?
beta-amyloid precursor protein APP + H2O
beta-amyloid protein + beta-amyloid precursor protein pre-peptide
-
cleavage at KLVF-/-FAED and at LVFF-/-AEDV, and with low activity at EVKM-/-DAEF
-
-
?
additional information
?
-
the enzyme might be involved in Alzheimer's disease
-
-
?
additional information
?
-
-
the enzyme might be involved in Alzheimer's disease
-
-
?
additional information
?
-
-
BACE2 cleaves at the beta site and more efficiently at a different site within amyloid-beta precursor protein
-
-
?
additional information
?
-
-
the enzyme is involved in Alzheimer's disease
-
-
?
additional information
?
-
-
the enzyme might be involved in Alzheimer's disease
-
-
?
additional information
?
-
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-N-(3-(3-amino-1-methyl-9-oxa-4-thia-2-azaspiro[5.5]undec-2-en-1-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
(R)-N-(3-(3-amino-5-methyl-9,9-dioxido-2,9-dithia-4-azaspiro[5.5]undec-3-en-5-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
(R)-N-(3-(3-amino-9,9-difluoro-5-methyl-2-thia-4-azaspiro[5.5]undec-3-en-5-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
(R)-N-(3-(7-amino-2,2-difluoro-9-methyl-6-thia-8-azaspiro[3.5]non-7-en-9-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(2,2,2-trifluoroethoxy)pyrazine-2-carboxamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(difluoromethyl)pyrazine-2-carboxamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-chloropicolinamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-cyanopicolinamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-fluoropicolinamide
-
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-methoxypyrazine-2-carboxamide
-
4-[2-(2,6-diethylpyridin-4-yl)-5-(pyrimidin-5-yl)phenyl]-1-methyl-4,5-dihydro-1H-imidazol-2-amine
-
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-N,5-dimethyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-N-methyl-5-[methyl(methylsulfonyl)amino]-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxohexan-2-yl]amino)-1-phenylbutan-2-yl]-N,5-dimethyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxohexan-2-yl]amino)-1-phenylbutan-2-yl]-N-methyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N'-[(2S,3R)-3-hydroxy-4-[(3-methoxybenzyl)amino]-1-phenylbutan-2-yl]-N,5-dimethyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N-(3-((4R,5R)-2-amino-5-methoxy-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
N-(3-((4S,5R)-2-amino-4-methyl-5-(tetrahydro-2H-pyran-4-yl)-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
N-(3-((4S,5R)-2-amino-4-methyl-5-phenyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
N-(3-((4S,5S)-2-amino-4-methyl-5-phenyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
-
N-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-5-methyl-N'-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-5-[methyl(methylsulfonyl)amino]-N'-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N-[(2S,3R)-3-hydroxy-4-[(3-methoxybenzyl)amino]-1-phenylbutan-2-yl]-5-[methyl(methylsulfonyl)amino]-N'-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
-
N-[2-[(4aR,6S,8aR)-2-amino-6-methyl-4,4a,5,6-tetrahydropyrano[3,4-d][1,3]thiazin-8a(8H)-yl]-1,3-thiazol-4-yl]-5-(difluoromethoxy)pyridine-2-carboxamide
-
N-[3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl]-5-chloropyridine-2-carboxamide
-
N-[3-[(4aS,5S,7aS)-2-amino-5-(trifluoromethyl)-4a,5-dihydro-4H-furo[3,4-d][1,3]thiazin-7a(7H)-yl]-4-fluorophenyl]-5-(1H-1,2,4-triazol-1-yl)pyrazine-2-carboxamide
-
N1-((2S,3R)-3-hydroxy-1-phenyl-4-((3-(trifluoromethyl)benzyl)amino)butan-2-yl)-N3,5-dimethyl-N3-((R)-1-phenylethyl)isophthalamide
-
N3-[(1S,2R)-1-benzyl-2-hydroxy-3-[[(1S,2S)-2-hydroxy-1-(isobutylcarbamoyl)pentyl]amino]propyl]-N1-methyl-N1-[(1R)-1-phenylpropyl]benzene-1,3-dicarboxamide
-
N3-[(1S,2R)-1-benzyl-2-hydroxy-3-[[(1S,2S)-2-hydroxy-1-(isobutylcarbamoyl)propyl]amino]propyl]-5-[methyl(methylsulfonyl)amino]-N1-[(1R)-1-phenylpropyl]benzene-1,3-dicarboxamide
-
[(1S,5S,6S)-3-amino-5-(2-fluoro-5-[(Z)-2-fluoro-2-[5-(prop-2-yn-1-yloxy)pyrazin-2-yl]ethenyl]phenyl)-5-methyl-2-thia-4-azabicyclo[4.1.0]hept-3-en-1-yl][(3R)-3-methylmorpholin-4-yl]methanone
-
2-(3-(imidazo[1,2-a]pyridin-2-yl)phenyl)-6-methoxy-1Hbenzo[d]imidazole
-
inhibitor of BACE1, EC 3.4.23.46. 150fold more effective on BACE1 than BACE2
6-fluoro-2-(3-(7-fluoroimidazo[1,2-a]pyridin-2-yl)phenyl)-1H-benzo[d]imidazole
-
inhibitor of BACE1, EC 3.4.23.46. 200fold more effective on BACE1 than BACE2
6-fluoro-2-(3-(imidazo[1,2-a]pyridin-2-yl)phenyl)-1H-benzo-[d]imidazole
-
inhibitor of BACE1, EC 3.4.23.46. 100fold more effective on BACE1 than BACE2
Glu-Val-Asn-Leu-CONH-Ala-Ala-Glu-Phe
-
inhibitors based on this structure, molecular size is substantially reduced while maintaining comparable enzyme inhibitory potencies
Lys-Thr-Glu-Glu-Ile-Ser-Glu-Val-Asn-Stat-Val-Ala-Glu-Phe
-
P10-P40 StatVal, beta-secretase inhibitor
N-{(1S,2R)-1-benzyl-2-hydroxy-3-[(3-methylbenzyl)amino]propyl}dibenzo[b,f]oxepine-10-carboxamide
-
hydroxyethylamine transition-state inhibitor, binding structure at the active site, interaction mode
additional information
-
M617V mutation in amyloid-beta precursor protein inhibits BACE2 beta-site cleavage
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000001
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-N,5-dimethyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.0000805
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-N-methyl-5-[methyl(methylsulfonyl)amino]-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.000038
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxohexan-2-yl]amino)-1-phenylbutan-2-yl]-N,5-dimethyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.000031
N'-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxohexan-2-yl]amino)-1-phenylbutan-2-yl]-N-methyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.00001402
N'-[(2S,3R)-3-hydroxy-4-[(3-methoxybenzyl)amino]-1-phenylbutan-2-yl]-N,5-dimethyl-N-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.0001828
N-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-5-methyl-N'-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.0000146
N-[(2S,3R)-3-hydroxy-4-([(2S,3S)-3-hydroxy-1-[(2-methylpropyl)amino]-1-oxobutan-2-yl]amino)-1-phenylbutan-2-yl]-5-[methyl(methylsulfonyl)amino]-N'-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.000137
N-[(2S,3R)-3-hydroxy-4-[(3-methoxybenzyl)amino]-1-phenylbutan-2-yl]-5-[methyl(methylsulfonyl)amino]-N'-[(1R)-1-phenylethyl]benzene-1,3-dicarboxamide
pH and temperature not specified in the publication
0.003224
2-(3-(imidazo[1,2-a]pyridin-2-yl)phenyl)-6-methoxy-1Hbenzo[d]imidazole
-
pH 4.5, 25Ā°C
0.003568
6-fluoro-2-(3-(7-fluoroimidazo[1,2-a]pyridin-2-yl)phenyl)-1H-benzo[d]imidazole
-
pH 4.5, 25Ā°C
0.003081
6-fluoro-2-(3-(imidazo[1,2-a]pyridin-2-yl)phenyl)-1H-benzo-[d]imidazole
-
pH 4.5, 25Ā°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000631
(R)-N-(3-(3-amino-1-methyl-9-oxa-4-thia-2-azaspiro[5.5]undec-2-en-1-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00209
(R)-N-(3-(3-amino-5-methyl-9,9-dioxido-2,9-dithia-4-azaspiro[5.5]undec-3-en-5-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00166
(R)-N-(3-(3-amino-9,9-difluoro-5-methyl-2-thia-4-azaspiro[5.5]undec-3-en-5-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000129
(R)-N-(3-(7-amino-2,2-difluoro-9-methyl-6-thia-8-azaspiro[3.5]non-7-en-9-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000316
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(2,2,2-trifluoroethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000102
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(difluoromethyl)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000078
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.0000087
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-chloropicolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000021
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-cyanopicolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000014
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-fluoropicolinamide
Homo sapiens
pH and temperature not specified in the publication
0.000085
(S)-N-(3-(2-amino-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-methoxypyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000251
N-(3-((4R,5R)-2-amino-5-methoxy-4-methyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000074
N-(3-((4S,5R)-2-amino-4-methyl-5-(tetrahydro-2H-pyran-4-yl)-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000028
N-(3-((4S,5R)-2-amino-4-methyl-5-phenyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000013
N-(3-((4S,5S)-2-amino-4-methyl-5-phenyl-5,6-dihydro-4H-1,3-thiazin-4-yl)-4-fluorophenyl)-5-(fluoromethoxy)pyrazine-2-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00332
2-(3-(imidazo[1,2-a]pyridin-2-yl)phenyl)-6-methoxy-1Hbenzo[d]imidazole
Homo sapiens
-
pH 4.5, 25Ā°C
0.00367
6-fluoro-2-(3-(7-fluoroimidazo[1,2-a]pyridin-2-yl)phenyl)-1H-benzo[d]imidazole
Homo sapiens
-
pH 4.5, 25Ā°C
0.00317
6-fluoro-2-(3-(imidazo[1,2-a]pyridin-2-yl)phenyl)-1H-benzo-[d]imidazole
Homo sapiens
-
pH 4.5, 25Ā°C
0.000041
Lys-Thr-Glu-Glu-Ile-Ser-Glu-Val-Asn-Stat-Val-Ala-Glu-Phe
Homo sapiens
-
pH 4.5, 37Ā°C, substrate concentration 0.015 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transcription control at two sites, tissue-specific expression, overview
additional information
-
low mRNA level in the brain compared with other organs, 10fold lower mRNA level in the brain compared with BACE1
-
postmortem samples of fetal brain at 18-19 weeks of gestational age and of frontal cortex of adult brains
-
samples from frontal cortex of both Alzheimer's disease-affected individuals and age-matched controls. Samples show substantial total amounts of BACE2 protein and enzymatic activity. BACE2 activity does not change significantly in the brain of patients with Alzheimer's disease, and is not related to amyloid beta-peptide concentration
-
in normal human pancreas, BACE2 expression is restricted to beta-cells. BACE2 colocalizes with clathrin-coated vesicles of the plasma membrane in MIN6 cells. Pharmacological inhibition of BACE2 results in increased BACE2 content in clathrin-coated vesicles, reduced insulin internalization rate, decreased in insulin receptor beta-subunit at the plasma membrane and increase in the Golgi apparatus, and a significant reduction in insulin gene expression. Similar results are obtained after specific BACE2 silencing in MIN6 cells. Data point to a role for BACE2 in the insulin receptor-beta subunit trafficking and insulin signaling
additional information
-
tissue-type specific expression, BACE2 expression is high in peripheral tissues and in brain regions including the postcentral gyrus and temporal lobes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the key step in the generation of Abeta is cleavage of APP by beta-secretase
physiological function
physiological function
-
BACE2 colocalizes with clathrin-coated vesicles of the plasma membrane in MIN6 cells. Pharmacological inhibition of BACE2 results in increased BACE2 content in clathrin-coated vesicles, reduced insulin internalization rate, decreased in insulin receptor beta-subunit at the plasma membrane and increase in the Golgi apparatus, and a significant reduction in insulin gene expression. Similar results are obtained after specific BACE2 silencing in MIN6 cells. Data point to a role for BACE2 in the insulin receptor-beta subunit trafficking and insulin signaling
physiological function
-
in a mouse model of in vivo BACE2 overexpression, BACE2 is not involved in the amyloidogenic pathway, cognitive dysfunction or cholinergic degeneration. Transgenic BACE2 animals show increased anxiety-like behaviour along with increased numbers of noradrenergic neurones in locus coeruleus
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BACE2_HUMAN
518
1
56180
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
60000
-
glycosylated, SDS-PAGE, present in muscle biopsies, but not in cultured fibers
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
modeling the tertiary structure, domain structure, overview
additional information
-
modeling the tertiary structure, domain structure, overview
additional information
-
amino acid sequence and domain structure, comparison to BACE1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
proteolytic modification
proteolytic modification
-
autoactivation in an acidic solution with cleavage of the own propeptide within the sequence Gly-Leu-Ala-Leu--/-Ala-Leu-Glu-Pro
proteolytic modification
-
autoactivation of the inactive zymogen by cleavage of the propeptide
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
evolutionary trace analysis identifies group-specific residues in the ligand binding sites of BACE1, EC 3.4.23.46, and BACE2.The residues are Pro70, Ile110, Ile126, andAsn233 of BACE1 substituting Lys86, Leu126, Leu142, and Leu246 of BACE2, respectively.These group-specific residues would be the reason for cleavage site selectivity in BACE1 and BACE2 biological function
in complex with inhibitor N3-[(1S,2R)-1-benzyl-2-hydroxy-3-[[(1S,2S)-2-hydroxy-1-(isobutylcarbamoyl)propyl]amino]propyl]-5-[methyl(methylsulfonyl)amino]-N1 -[(1R)-1-phenylpropyl]benzene-1,3-dicarboxamide
purified N- and C-terminally truncated BACE2, residues Ala13-Ala398, in complex with hydroxyethylamine transition-state inhibitor, 0.001 ml of 8.8 mg/ml protein in 10 mM Tris-HCl, pH 6.8, 350 mM NaCl, 2 mM inhibitor, and 2% v/v DMSO, 20Ā°C, is mixed with 0.001 ml of reservoir solution containing 16% w/v PEG 8000, 100 mM CaCl2, and 5% v/v glycerol, equilibration against 0.6 ml reservoir solution, six to eight weeks, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R310Lys
-
mutation interferes with the ability of the enzyme to cleave at the beta site of amyloid-beta precursor protein, but not at their respective cleavage sites internal to amyloid-beta protein
additional information
-
construction of an N- and C-terminally truncated BACE2 lacking the transmembrane and the cytoplasmic domains
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the encoding gene is located on chromosome 21 in the Down syndrome critical region
coexpressed with the Swedish mutant of APP in 20E2 cells, expressed as GFP-fusion protein using lentivirus
-
DNA and amino acid sequence analysis, 5'-flanking region analysis, BACE2 mapping to chromosome 21q22.3, expression analysis, sequence comparison to BACE1
-
DNA and amino acid sequence analysis, expression analysis, sequence comparison to BACE1, functional expression in primary rat cortical cell cultures
-
expressed together with full length IL-IR2 or truncated form DELTA322-IL-1R2 in HEK 293 cells
-
expression of the wild-type and mutated zymogens in Escherichia coli strain BL21(DE3) in inclusion bodies, followed by refolding and autoactivation
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
BACE2 mRNA levels are downregulated at 6, 12, and 24 h exposure to 0.01 mM AlCl3 and 0.002 mM amyloid beta peptide
BACE2 mRNA levels are significantly increased after 1 and 3 h exposure to 0.01 mM AlCl3 and 0.002 mM amyloid beta peptide
neither treatment with 0.002 mM of the Abeta(25-35) fragment nor with 0.01 mM AlCl3 alone influences BACE2 gene mRNA after 24 h
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding of recombinant zymogen from Escherichia coli strain BL21(DE3) inclusion bodies followed by autoactivation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
the enzyme is a potential target for development of inhibitors in Alzheimer's disease therapy and treatment of Down syndrome
drug development
-
therapeutic interventions that potentiate BACE2 may prevent AlzheimerĀs disease
medicine
-
samples from frontal cortex of both Alzheimer's disease-affected individuals and age-matched controls show substantial total amounts of BACE2 protein and enzymatic activity. BACE2 activity does not change significantly in the brain of patients with Alzheimer's disease, and is not related to amyloid beta-peptide concentration
medicine
in patients with preclinical to late-stage Alzheimer's disease, including amnestic mild cognitive impairment, and age-matched controls, cases of frontotemporal dementia, and Down's syndrome, BACE2 protein and enzymatic activity increase as early as preclinical Alzheimer's disease and are found in neurons and astrocytes. Although the levels of total BACE2 mRNA are unchanged, the mRNA for BACE2 splice form C (missing exon 7) increases in parallel with BACE2 protein and activity. BACE1 and BACE2 are strongly correlated with each other at all levels. BACE2 is also elevated in frontotemporal dementia but not in Down's syndrome, even in patients with substantial amyloid beta deposition
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Farzan, M.; Schnitzler, C.E.; Vasilieva, N.; Leung, D.; Choe, H.
BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein
Proc. Natl. Acad. Sci. USA
97
9712-9717
2000
Homo sapiens
Fluhrer, R.; Capell, A.; Westmeyer, G.; Willem, M.; Hartung, B.; Condron, M.M.; Teplow, D.B.; Haass, C.; Walter, J.
A non-amyloidogenic function of BACE-2 in the secretory pathway
J. Neurochem.
81
1011-1020
2002
Homo sapiens
Ghosh, A.K.; Bilcer, G.; Harwood, C.; Kawahama, R.; Shin, D.; Hussain, K.A.; Hong, L.; Loy, J.A.; Nguyen, C.; Koelsch, G.; Ermolieff, J.; Tang, J.
Structure-based design: potent inhibitors of human brain memapsin 2 (beta-secretase)
J. Med. Chem.
44
2865-2868
2001
Homo sapiens
Kim, Y.T.; Downs, D.; Wu, S.; Dashti, A.; Pan, Y.; Zhai, P.; Wang, X.; Zhang, X.C.; Lin, X.
Enzymic properties of recombinant BACE2
Eur. J. Biochem.
269
5668-5677
2002
Homo sapiens
Motonaga, K.; Itoh, M.; Becker, L.E.; Goto, Y.I.; Takashima, S.
Elevated expression of beta-site amyloid precursor protein cleaving enzyme 2 in brains of patients with Down syndrome
Neurosci. Lett.
326
64-66
2002
Homo sapiens
Solans, A.; Estivill, X.; de La Luna, S.
A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein beta-secretase
Cytogenet. Cell Genet.
89
177-184
2000
Homo sapiens, Homo sapiens (Q9Y5Z0)
Turner, R.T.3rd.; Loy, J.A.; Nguyen, C.; Devasamudram, T.; Ghosh, A.K.; Koelsch, G.; Tang, J.
Specificity of memapsin 1 and its implications on the design of memapsin 2 (beta-secretase) inhibitor selectivity
Biochemistry
41
8742-8746
2002
Homo sapiens
Vattemi, G.; Engel, W.K.; McFerrin, J.; Pastorino, L.; Buxbaum, J.D.; Askanas, V.
BACE1 and BACE2 in pathologic and normal human muscle
Exp. Neurol.
179
150-158
2003
Homo sapiens
Hussain, I.; Powell, D.J.; Howlett, D.R.; Chapman, G.A.; Gilmour, L.; Murdock, P.R.; Tew, D.G.; Meek, T.D.; Chapman, C.; Schneider, K.; Ratcliffe, S.J.; Tattersall, D.; Testa, T.T.; Southan, C.; Ryan, D.M.; Simmons, D.L.; Walsh, F.S.; Dingwall, C.; Christie, G.
ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site
Mol. Cell. Neurosci.
16
609-619
2000
Homo sapiens (Q9Y5Z0)
Tang, J.; Koelsch, G.
Memapsin 1
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
64-66
2004
Homo sapiens
-
Ostermann, N.; Eder, J.; Eidhoff, U.; Zink, F.; Hassiepen, U.; Worpenberg, S.; Maibaum, J.; Simic, O.; Hommel, U.; Gerhartz, B.
Crystal structure of human BACE2 in complex with a hydroxyethylamine transition-state inhibitor
J. Mol. Biol.
355
249-261
2006
Homo sapiens
Lahiri, D.K.; Maloney, B.; Ge, Y.W.
Functional domains of the BACE1 and BACE2 promoters and mechanisms of transcriptional suppression of the BACE2 promoter in normal neuronal cells
J. Mol. Neurosci.
29
65-80
2006
Homo sapiens
Maloney, B.; Ge, Y.W.; Greig, N.H.; Lahiri, D.K.
Characterization of the human beta-secretase 2 (BACE2) 5-flanking region: identification of a 268-bp region as the basal BACE2 promoter
J. Mol. Neurosci.
29
81-99
2006
Homo sapiens
Chou, K.C.
Insights from modeling the tertiary structure of human BACE2
J. Proteome Res.
3
1069-1072
2004
Homo sapiens (Q9Y5Z0), Homo sapiens
Stockley, J.H.; O'Neill, C.
The proteins BACE1 and BACE2 and beta-secretase activity in normal and Alzheimers disease brain
Biochem. Soc. Trans.
35
574-576
2007
Homo sapiens
Stockley, J.H.; Ravid, R.; ONeill, C.
Altered beta-secretase enzyme kinetics and levels of both BACE1 and BACE2 in the Alzheimers disease brain
FEBS Lett.
580
6550-6560
2006
Homo sapiens, Rattus norvegicus
Cheon, M.S.; Dierssen, M.; Kim, S.H.; Lubec, G.
Protein expression of BACE1, BACE2 and APP in Down syndrome brains
Amino Acids
35
339-343
2007
Homo sapiens
Sun, X.; He, G.; Song, W.
BACE2, as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimers disease in Down syndrome
FASEB J.
20
1369-1376
2006
Homo sapiens
Kuhn, P.H.; Marjaux, E.; Imhof, A.; De Strooper, B.; Haass, C.; Lichtenthaler, S.F.
Regulated intramembrane proteolysis of the interleukin-1 receptor II by alpha-, beta-, and gamma-secretase
J. Biol. Chem.
282
11982-11995
2007
Homo sapiens
Venugopal, C.; Demos, C.M.; Rao, K.S.; Pappolla, M.A.; Sambamurti, K.
beta-Secretase: structure, function, and evolution
CNS Neurol. Disord. Drug Targets
7
278-294
2008
Homo sapiens
Castorina, A.; Tiralongo, A.; Giunta, S.; Carnazza, M.L.; Scapagnini, G.; DAgata, V.
Early effects of aluminum chloride on beta-secretase mRNA expression in a neuronal model of ss-amyloid toxicity
Cell Biol. Toxicol.
26
367-377
2010
Homo sapiens (Q9Y5Z0)
Ahmed, R.R.; Holler, C.J.; Webb, R.L.; Li, F.; Beckett, T.L.; Murphy, M.P.
BACE1 and BACE2 enzymatic activities in Alzheimers disease
J. Neurochem.
112
1045-1053
2010
Homo sapiens
Vassar, R.; Kovacs, D.M.; Yan, R.; Wong, P.C.
The beta-secretase enzyme BACE in health and Alzheimers disease: regulation, cell biology, function, and therapeutic potential
J. Neurosci.
29
12787-12794
2009
Homo sapiens
Casas, S.; Casini, P.; Piquer, S.; Altirriba, J.; Soty, M.; Cadavez, L.; Gomis, R.; Novials, A.
BACE2 plays a role in the insulin receptor trafficking in pancreatic beta-cells
Am. J. Physiol. Endocrinol. Metab.
299
E1087-E1095
2010
Homo sapiens
Azkona, G.; Amador-Arjona, A.; Obradors-Tarrago, C.; Varea, E.; Arque, G.; Pinacho, R.; Fillat, C.; De La Luna, S.; Estivill, X.; Dierssen, M.
Characterization of a mouse model overexpressing beta-site APP-cleaving enzyme 2 reveals a new role for BACE2
Genes Brain Behav.
9
160-172
2010
Homo sapiens
Al-Tel, T.; Semreen, M.; Al-Qawasmeh, R.; Schmidt, M.; El-Awadi, R.; Ardah, M.; Zaarour, R.; Rao, S.; El-Agnaf, O.
Design, synthesis, and qualitative structure-activity evaluations of novel beta-secretase inhibitors as potential Alzheimers drug leads
J. Med. Chem.
54
8373-8385
2011
Homo sapiens
Holler, C.; Webb, R.; Laux, A.; Beckett, T.; Niedowicz, D.; Ahmed, R.; Liu, Y.; Simmons, C.; Dowling, A.; Spinelli, A.; Khurgel, M.; Estus, S.; Head, E.; Hersh, L.; Murphy, M.
BACE2 expression increases in human neurodegenerative disease
Am. J. Pathol.
180
337-350
2012
Homo sapiens (Q9Y5Z0), Homo sapiens
Abdul-Hay, S.O.; Sahara, T.; McBride, M.; Kang, D.; Leissring, M.A.
Identification of BACE2 as an avid beta-amyloid-degrading protease
Mol. Neurodegener.
7
46
2012
Homo sapiens (Q9Y5Z0)
Mirsafian, H.; Mat Ripen, A.; Merican, A.F.; Bin Mohamad, S.
Amino acid sequence and structural comparison of BACE1 and BACE2 using evolutionary trace method
ScientificWorldJournal
2014
482463
2014
Homo sapiens (Q9Y5Z0)
Ghosh, A.K.; Reddy, B.S.; Yen, Y.C.; Cardenas, E.; Rao, K.V.; Downs, D.; Huang, X.; Tang, J.; Mesecar, A.D.
Design of potent and highly selective inhibitors for human beta-secretase 2 (memapsin 1), a target for type 2 diabetes
Chem. Sci.
7
3117-3122
2016
Homo sapiens (Q9Y5Z0), Homo sapiens
Ghosh, A.K.; Brindisi, M.; Yen, Y.C.; Lendy, E.K.; Kovela, S.; Cardenas, E.L.; Reddy, B.S.; Rao, K.V.; Downs, D.; Huang, X.; Tang, J.; Mesecar, A.D.
Highly selective and potent human beta-secretase 2 (BACE2) inhibitors against type 2 diabetes design, synthesis, X-ray structure and structure-activity relationship studies
ChemMedChem
14
545-560
2019
Homo sapiens (Q9Y5Z0), Homo sapiens
Fujimoto, K.; Matsuoka, E.; Asada, N.; Tadano, G.; Yamamoto, T.; Nakahara, K.; Fuchino, K.; Ito, H.; Kanegawa, N.; Moechars, D.; Gijsen, H.J.M.; Kusakabe, K.I.
Structure-based design of selective beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitors targeting the flap to gain selectivity over BACE2
J. Med. Chem.
62
5080-5095
2019
Homo sapiens (Q9Y5Z0)
EXTERNAL LINKS (specific for EC-Number 3.4.23.45)
Transporter Classification Database (TCDB): 8.A.32.1.2, 8.A.32.1.3
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