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D-Asp-L-Ala-L-Glu-L-Phe-L-Arg-L-His-D-Asp-L-Ser-Gly-L-Tyr + H2O
?
-
-
-
-
?
DAEFRH-(D-Asp)-GSY + H2O
DAEFRH-(D-Asp) + GSY
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synthetic Abeta peptide. No cleavage of the D-Aspcontaining Abeta peptide, paenidase I and II. Paenidases specifically recognize internal D-Asp residues and hydrolyze them on the COOH side
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-
?
L-Thr-L-Val-L-Leu-D-alpha-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg + H2O
?
-
-
-
-
?
succinyl-D-Asp-4-methylcoumaryl-7-amide + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
succinyl-D-Asp-7-amido-4-methylcoumarin + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
succinyl-D-Asp-alpha-4-methylcoumaryl-7-amide + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-D-Asp-p-nitroanilide + H2O
succinyl-D-Asp + p-nitroaniline
[D-Asp]AEFRH[D-Asp]SGY + H2O
[D-Asp]AEFRHX + SGY
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the D-Abeta1-10 peptide is degraded at D-Asp7 and two peptides are produced [D-Asp]AEFRHX and SGY. X is not identified in this study. L-Abeta110 peptide could not be degraded by this enzyme
-
-
?
[D-Asp]AEFRH[D-Asp]SGY + H2O
[D-Asp]AEFRH[D-Asp] + SGY
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the D-Abeta1-10 peptide is degraded at D-Asp7 and two peptides are produced [D-Asp]AEFRHX and SGY. X is not identified in this study. L-Abeta110 peptide could not be degraded by this enzyme
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-
?
additional information
?
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succinyl-D-Asp-4-methylcoumaryl-7-amide + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-D-Asp-4-methylcoumaryl-7-amide + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
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paenidases specifically recognize internal D-Asp residues and hydrolyze them on the COOH side
-
-
?
succinyl-D-Asp-7-amido-4-methylcoumarin + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
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-
-
-
?
succinyl-D-Asp-7-amido-4-methylcoumarin + H2O
succinyl-D-Asp + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-D-Asp-p-nitroanilide + H2O
succinyl-D-Asp + p-nitroaniline
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paenidases specifically recognize internal D-Asp residues and hydrolyze them on the COOH side
-
-
?
succinyl-D-Asp-p-nitroanilide + H2O
succinyl-D-Asp + p-nitroaniline
-
-
-
?
additional information
?
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the enzyme may serve as a scavenger against accumulation of racemized proteins in aging
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-
?
additional information
?
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no activity with succinyl-L-Asp-7-amido-4-methylcoumarin, L-Thr-L-Val-L-Leu-L-alpha-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg, L-Thr-L-Val-L-Leu-D-beta-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg and L-Thr-L-Val-L-Leu-D-beta-Asp-L-Ser-Gly-L-Ile-L-Ser-L-Glu-L-Val-L-Arg
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-
?
additional information
?
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the accumulation of D-isomers of aspartic acid in proteins during aging is involved in the pathogenesis of Alzheimers disease, cataracts, and arteriosclerosis. The enzyme may serve as a scavenger against accumulation of racemized proteins in aging
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-
?
additional information
?
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the enzyme may serve as a scavenger against accumulation of racemized proteins in aging
-
-
?
additional information
?
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no activity with acetyl-Tyr-Val-Ala-Asp-4-methylcoumaryl-7-amide, acetyl-Asp-Glu-Val-Asp-4-methylcoumaryl-7-amide, succinyl-Gly-Pro-Leu-Gly-Pro-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide, Leu-4-methylcoumaryl-7-amide, succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Leu-Leu-Glu-4-methylcoumaryl-7-amide, Ala-Ala-Phe-4-methylcoumaryl-7-amide, succinyl-Ala-[D-Ser]-4-methylcoumaryl-7-amide, succinyl-[D-Ser]-4-methylcoumaryl-7-amide
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-
?
additional information
?
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no activity with acetyl-Tyr-Val-Ala-Asp-4-methylcoumaryl-7-amide, acetyl-Asp-Glu-Val-Asp-4-methylcoumaryl-7-amide, succinyl-Gly-Pro-Leu-Gly-Pro-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide, Leu-4-methylcoumaryl-7-amide, succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide, benzyloxycarbonyl-Leu-Leu-Glu-4-methylcoumaryl-7-amide, Ala-Ala-Phe-4-methylcoumaryl-7-amide, succinyl-Ala-[D-Ser]-4-methylcoumaryl-7-amide, succinyl-[D-Ser]-4-methylcoumaryl-7-amide
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-
?
additional information
?
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no activity with: acetyl-L-Asp-p-nitroanilide, D-Asp-p-nitroanilide, A-Ala-p-nitroanilide, D-Leu-p-nitroanilide, D-Phe-p-nitroanilide, L-Asp-p-nitroanilide, L-Ala-p-nitroanilide, L-Leu-p-nitroanilide, L-Phe-p-nitroanilide, L-Arg-p-nitroanilide, L-Glu-p-nitroanilide, Gly-p-nitroanilide, L-His-p-nitroanilide, L-Ile-p-nitroanilide, L-Lys-p-nitroanilide, L-Met-p-nitroanilide, L-Pro-p-nitroanilide, L-Val-p-nitroanilide, p-nitroanilide, succinyl-L-Ala-L-Pro-L-Ala, succinyl-L-Ala-L-Ala-L-Ala-p-nitroanilide, L-Pyr-p-nitroanilide, Arg-4-methylcoumaryl-7-amide, benzoyl-Arg-4-methylcoumaryl-7-amide, tert-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide, Pro-Phe-Arg-4-methylcoumaryl-7-amide, acetyl-Tyr-val-Ala-Asp-4-methylcoumaryl-7-amide, acetyl-ASp-GLu-Val-Asp-4-methylcoumaryl-7-amide, acetyl-Val-Glu-Ile-Asp-4-methylcoumaryl-7-amide
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-
?
additional information
?
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enzyme specifically recognizes an internal D-Asp residue to cleave [D-Asp]-X peptide bonds
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?
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1,10-phenanthroline
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0.1 mM, 8.3% inhibition
Aprotinin
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0.1 mM, 14% inhibition
benzoyl-Arg-His-D-Asp-CH2Cl
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1 mM, about 70% inhibition of paenidase I and II
benzoyl-Arg-His-[D-Asp]-CH2Cl
0.1 mM, 48% residual activity
benzoyl-L-Arg-L-His-D-Asp-CH2Cl
-
0.003 mM, 50% inhibition
biotinyl-(epsilon-aminocaproic acid)-L-Arg-L-His-D-Asp-CH2Cl
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Co2+
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1.0 mM, 31% inhibition of paenidase I, 46% inhibition of paenidase II
diisopropyl fluorophosphate
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at 0.5 mM, 15.5% inhibition
leupeptin
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0.03 mM, 8.5% inhibition
NEM
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0.1 mM, about 10% inhibition
pepstatin
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0.01 mg/ml, about 50% inhibition of paenidase I and II
phosphoramidon
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0.01 mM, 9.9% inhibition
lactacystin
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Mn2+
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1.0 mM MnCl2, 31% inhibition of paenidase I, 60% inhibition of paenidase II
Mn2+
0.1 mM, 68% residual activity
pepstatin A
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0.01 mM,5.3% inhibition
pepstatin A
-
0.01 mM, 5.3% inhibition
Zn2+
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0.25 mM ZnCl2, 98% inhibition of paenidase I and II
Zn2+
0.1 mM, 46% residual activity
additional information
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no inhibition: N-p-tosyl-L-phenylalanine chloromethyl ketone, N-p-tosyl-L-lysine chloromethyl ketone, phenylmethylsulfonyl fluoride, trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane, L-alanyl-L-alanyl-L-phenylalanyl-chloromethane, chymostatin, EDTA, epoxomicin, N-acetyl-L-leucyl-L-leucyl-norleucinal
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additional information
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no inhibition: N-p-tosyl-L-phenylalanine chloromethyl ketone, N-p-tosyl-L-lysine chloromethyl ketone, phenylmethylsulfonyl fluoride, trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane, L-alanyl-L-alanyl-L-phenylalanyl-chloromethane, chymostatin, EDTA
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additional information
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no inhibition: iodoacetic acid, p-chloromercuribenzoate, EDTA, 1,10-phenanthroline, amastatin, antipain, diisopropylfluorophosphate, soybean trypsin inhibitor
-
additional information
not inhibitory: pepstatin, Co2+
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Kinouchi, T.; Ishiura, S.; Mabuchi, Y.; Urakami-Manaka, Y.; Nishio, H.; Nishiuchi, Y.; Tsunemi, M.; Takada, K.; Watanabe, M.; Ikeda, M.; Matsui, H.; Tomioka, S.; Kawahara, H.; Hamamoto, T.; Suzuki, K.; Kagawa, Y.
Mammalian D-aspartyl endopeptidase: a scavenger for noxious racemized proteins in aging
Biochem. Biophys. Res. Commun.
314
730-736
2004
Oryctolagus cuniculus, Mus musculus, no activity in Caenorhabditis elegans, no activity in Saccharomyces cerevisiae, no activity in Escherichia coli
brenda
Kinouchi, T.; Nishio, H.; Nishiuchi, Y.; Tsunemi, M.; Takada, K.; Hamamoto, T.; Kagawa, Y.; Fujii, N.
Isolation and characterization of mammalian D-aspartyl endopeptidase
Amino Acids
32
79-85
2007
Oryctolagus cuniculus, Mus musculus
brenda
Sakai-Kato, K.; Kinouchi, T.; Fujii, N.; Imai, K.; Utsunomiya-Tate, N.
Screening system for D-Asp-containing proteins using D-aspartyl endopeptidase and two-dimensional gel electrophoresis
Amino Acids
36
125-129
2009
Oryctolagus cuniculus
brenda
Takahashi, S.; Ogasawara, H.; Hiwatashi, K.; Hori, K.; Hata, K.; Tachibana, T.; Itoh, Y.; Sugiyama, T.
Paenidase, a novel D-aspartyl endopeptidase from Paenibacillus sp. B38: purification and substrate specificity
J. Biochem.
139
197-202
2006
Paenibacillus sp.
brenda
Kinouchi, T.; Fujii, N.
Structural consideration of mammalian D-aspartyl endopeptidase
Chem. Biodivers.
7
1403-1407
2010
Mus musculus
brenda
Kinouchi, T.; Fujii, N.; Fujii, N.
Substrate stereoselectivity of mammalian D-aspartyl endopeptidase
J. Chromatogr. B
879
3349-3352
2011
Mus musculus
brenda
Nirasawa, S.; Nakahara, K.; Takahashi, S.
Cloning and characterization of the novel D-aspartyl endopeptidase, paenidase, from Paenibacillus sp. B38
J. Biochem.
164
103-112
2018
Paenibacillus sp. B38 (A0A2Z6BCG6)
brenda