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2-(2-[(4-methylbenzene-1-sulfonyl)amino]ethyl)-1,3-dioxo-2,3-dihydro-1H-benzo[de]isoquinolin-6-yl 2-[(leucylamino)methyl]piperidine-1-carboxylate + H2O
N-[2-(6-hydroxy-1,3-dioxo-6,6a-dihydro-1H-benzo[de]isoquinolin-2(3H)-yl)ethyl]-4-methylbenzene-1-sulfonamide + hexahydroimidazo[1,5-a]pyridin-3(2H)-one + 2-amino-4-methylpentanoic acid
two-photon fluorescent probe SNCL, can be applied for monitoring of the activity in living cells and tissues
-
-
?
AAEAAG-NH2 + H2O
L-Ala + AEAAG-NH2
-
-
-
-
?
AAVVAAG-NH2 + H2O
L-Ala + AVVAAG-NH2
-
-
-
-
?
AEAA-NH2 + H2O
L-Ala + EAA-NH2
-
-
-
-
?
Ala 2-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
?
Ala 4-nitroanilide + H2O
Ala + 4-nitroaniline
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
Ala-Ala-Pro-Tyr-Lys-amide + H2O
Ala + Ala-Pro-Tyr-Lys-amide
Ala-beta-naphthylamide + H2O
Ala + beta-naphthylamine
-
-
-
?
Arg 2-naphthylamide + H2O
Arg + 2-naphthylamine
-
-
-
?
Arg 4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
-
?
Asp 2-naphthylamide + H2O
Asp + 2-naphthylamine
-
very slight activity
-
?
Asp-4-nitroanilide + H2O
Asp + 4-nitroaniline
-
-
-
?
AYWANATRSG-D-Ala + H2O
L-Ala + AYWANATRSG-D-Ala
-
-
-
-
?
AYWANATRSGA + H2O
L-Ala + YWANATRSGA
-
high activity compared to other peptide substrates
-
-
?
azocasein + H2O
protein fragments of azocasein of MW 71 kDa, 83 kDa, and 22 kDa
-
-
-
-
?
Cystinyl 4-nitroanilide + H2O
Cystine + 4-nitroaniline
-
-
-
?
DRVYIHPFHL + H2O
L-Asp + L-Arg + VYIHPFHL
-
angiotensin I
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
EAA-NH2 + H2O
L-Glu + AA-NH2
-
-
-
-
?
EFAPGNYPAD + H2O
L-Glu + FAPGNYPAD
-
low activity compared to other peptide substrates
-
-
?
EFAPGNYPAK + H2O
L-Glu + FAPGNYPAK
-
low activity compared to other peptide substrates
-
-
?
EFAPGNYPAL + H2O
L-Glu + FAPGNYPAL
-
high activity compared to other peptide substrates
-
-
?
GDRIYVH + H2O
?
-
-
-
-
?
Glu 4-nitroanilide + H2O
Glu + 4-nitroaniline
-
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
Glu-Ala-Pro-Tyr-Lys-amide + H2O
Glu + Ala-Pro-Tyr-Lys-amide
Gly 4-nitroanilide + H2O
Gly + 4-nitroaniline
-
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
Gly-Ala-Pro-Tyr-Lys-amide + H2O
Gly + Ala-Pro-Tyr-Lys-amide
Gly-Leu-Tyr + H2O
Gly + Leu-Tyr
-
-
-
-
?
HSDAVFTDNYTRLRKQMAVKKYLNSILN + H2O
His + SDAVFTDNYTRLRKQM + AVKKYLN + SILN
-
protein VIP
-
-
?
Ile-4-nitroanilide + H2O
Ile + 4-nitroaniline
-
-
-
?
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
L-Ala-Ala-Pro-Leu-4-nitroanilide + H2O
L-Ala-Ala-Pro-Leu + 4-nitroaniline
-
-
-
-
?
L-Ala-Gly + H2O
L-Ala + Gly
-
-
-
-
?
L-Ala-Gly-Gly + H2O
?
-
-
-
-
?
L-Ala-Gly-Gly ethyl ester + H2O
L-Ala + Gly-Gly ethyl ester
-
-
-
-
?
L-Ala-L-Asp-L-Phe methyl ester + H2O
?
-
-
-
-
?
L-Ala-L-Leu + H2O
L-Ala + L-Leu
-
-
-
-
?
L-Ala-L-Thr + H2O
L-Ala + L-Thr
-
-
-
-
?
L-Ala-L-Thr-Gly methyl ester + H2O
?
-
-
-
-
?
L-Ala-L-Thr-L-Ala + H2O
?
-
-
-
-
?
L-Ala-L-Thr-L-Ala methyl ester + H2O
?
-
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
preferred substrate
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
L-Arg-L-Phe + H2O
L-Arg + L-Phe
-
-
-
-
?
L-Arg-p-nitroanilide + H2O
L-Arg + p-nitroaniline
-
-
-
-
?
L-Leu-2-naphthylamide + H2O
L-Leu + 2-naphthylamine
-
preferred substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
L-Leu-Gly + H2O
L-Leu + Gly
-
-
-
-
?
L-Leu-Gly-Gly + H2O
?
-
-
-
-
?
L-Leu-Gly-L-Leu + H2O
?
-
-
-
-
?
L-Leu-L-Ala + H2O
L-Leu + L-Ala
-
-
-
-
?
L-Leu-L-Leu + H2O
L-Leu + L-Leu
-
-
-
-
?
L-Leu-L-Phe + H2O
L-Leu + L-Phe
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
?
L-leucine-4-anisidide + H2O
L-leucine + anisidine
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-anilide + H2O
L-leucine + aniline
-
-
-
?
L-Lys-2-naphthylamide + H2O
L-Lys + 2-naphthylamine
-
low activity
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
L-Met-4-nitroanilide + H2O
L-Met + 4-nitroaniline
-
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
L-Met-L-Phe + H2O
L-Met + L-Phe
-
-
-
-
?
L-Phe-4-nitroanilide + H2O
L-Phe + 4-nitroaniline
-
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
L-Phe-Gly + H2O
L-Phe + Gly
-
-
-
-
?
L-Phe-Gly-Gly + H2O
?
-
-
-
-
?
L-Phe-L-Ala + H2O
L-Phe + L-Ala
-
-
-
-
?
L-Phe-L-Arg + H2O
L-Phe + L-Arg
-
-
-
-
?
L-Phe-L-Ile + H2O
L-Phe + L-Ile
-
-
-
-
?
L-Phe-L-Leu + H2O
L-Phe + L-Leu
-
-
-
-
?
L-Phe-L-Met + H2O
L-Phe + L-Met
-
-
-
-
?
L-Phe-L-Met-D-Arg-L-Phe-NH2 + H2O
L-Phe + L-Phe-L-Met-D-Arg-NH2
-
-
-
-
?
L-Phe-L-Met-L-Arg-L-Phe-NH2 + H2O
L-Phe + L-Phe-L-Met-L-Arg-NH2
-
bioactive molluscan cardioexcitatory neuropeptide
-
-
?
L-Phe-L-Phe + H2O
L-Phe + L-Phe
-
best substrate
-
-
?
L-Phe-L-Trp + H2O
L-Phe + L-Trp
-
-
-
-
?
L-Phe-L-Tyr + H2O
L-Phe + L-Tyr
-
-
-
-
?
L-Pro-4-nitroanilide + H2O
L-Pro + 4-nitroaniline
-
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Tyr-L-Phe + H2O
L-Tyr + L-Phe
-
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
-
low activity
-
-
?
Leu 2-naphthylamide + H2O
Leu + 2-naphthylamine
-
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
Leu-Ala-Pro-Tyr-Lys-amide + H2O
Leu + Ala-Pro-Tyr-Lys-amide
Leu-beta-naphthylamide + H2O
Leu + beta-naphthylamine
-
-
-
-
?
leucine enkephalin + H2O
?
-
recombinant enzyme, release of Tyr, Gly, Phe and Leu
-
?
LGGGGGGGGGGL + H2O
L-leucine + GGGGGGGGGGL
-
-
-
?
LGGGGGGGGGL + H2O
L-leucine + GGGGGGGGGL
-
-
-
?
LGGGL + H2O
L-leucine + GGGL
-
-
-
?
Lys 2-naphthylamide + H2O
Lys + 2-naphthylamine
-
-
-
?
Lys 4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
Met 4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
occludin + H2O
?
-
-
-
-
?
Phe 2-naphthylamide + H2O
Phe + 2-naphthylamine
-
-
-
?
Phe 4-nitroanilide + H2O
Phe + 4-nitroaniline
-
-
-
?
Phe-4-nitroanilide + H2O
Phe + 4-nitroaniline
-
-
?
Pro 2-naphthylamide + H2O
Pro + 2-naphthylamine
-
-
-
?
Pro 4-nitroanilide + H2O
Pro + 4-nitroaniline
-
-
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
low activity
-
?
Pro-Ala-Pro-Tyr-Lys-amide + H2O
Pro + Ala-Pro-Tyr-Lys-amide
QITANRELIQQEL + H2O
? + TANRELIQQEL
-
-
intermediate product TANRELIQQEL is further processed
-
?
QLESIINFEK + H2O
L-Gln + LESIINFEK
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKA + H2O
L-Gln + LESIINFEKA
-
high activity compared to other peptide substrates
-
-
?
QLESIINFEKD + H2O
L-Gln + LESIINFEKD
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKK + H2O
L-Gln + LESIINFEKK
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKL + H2O
L-Gln + LESIINFEKL
-
best peptide substrate
-
-
?
QLESIINFEKL-amide + H2O
L-Gln + LESIINFEKL-amide
-
high activity compared to other peptide substrates
-
-
?
QLESIINFEKR + H2O
L-Gln + LESIINFEKR
-
low activity compared to other peptide substrates
-
-
?
QLESIINFEKY + H2O
L-Gln + LESIINFEKY
-
high activity compared to other peptide substrates
-
-
?
QLESIINFELK + H2O
L-Gln + LESIINFELK
-
-
-
-
?
RPKPQQFFGLM + H2O
RPKPQ + QFF + GLM
-
substance P
-
-
?
RPPGFSPFR + H2O
Arg + PPGF + SPFR
-
bradykinin
-
-
?
S-Benzoyl-Cys 4-nitroanilide + H2O
S-Benzoyl-Cys + 4-nitroaniline
-
-
-
?
Ser 2-naphthylamide + H2O
Ser + 2-naphthylamine
-
-
-
?
SIINFEKL + H2O
L-Ser + IINFEKL
-
-
-
-
?
thionoleucine-4-anisidide + H2O
thionoleucine + anisidine
-
-
-
?
thionoleucine-S-anilide + H2O
thionoleucine + aniline
-
-
-
?
TTQRTRALV-NH2 + H2O
L-Thr + TQRTRALV-NH2
-
-
-
-
?
Tyr 2-naphthylamide + H2O
Tyr + 2-naphthylamine
-
-
-
?
Val 2-naphthylamide + H2O
Val + 2-naphthylamine
-
slight activity
-
?
Val 4-nitroanilide + H2O
Val + 4-nitroaniline
-
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
WEVYEKCALK + H2O
L-Trp + EVYEKCALK
-
-
-
-
?
WRVYEKCALK + H2O
L-Trp + RVYEKCALK
-
-
-
-
?
WRVYEKMALKC + H2O
L-Trp + RVYEKMALKC
-
-
-
-
?
additional information
?
-
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
low activity
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
best Xaa-4-nitroanilide substrate
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
best Xaa-4-nitroanilide substrate
-
?
Ala-Ala-Pro-Tyr-Lys-amide + H2O
Ala + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Ala-Ala-Pro-Tyr-Lys-amide + H2O
Ala + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
-
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
low activity
-
?
Glu-4-nitroanilide + H2O
Glu + 4-nitroaniline
-
-
-
?
Glu-Ala-Pro-Tyr-Lys-amide + H2O
Glu + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Glu-Ala-Pro-Tyr-Lys-amide + H2O
Glu + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
-
-
-
?
Gly-4-nitroanilide + H2O
Gly + 4-nitroaniline
-
-
-
?
Gly-Ala-Pro-Tyr-Lys-amide + H2O
Gly + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Gly-Ala-Pro-Tyr-Lys-amide + H2O
Gly + Ala-Pro-Tyr-Lys-amide
-
best pentapeptide substrate
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
high activity
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
preferred substrate, recombinant enzyme
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
substrate of the alpha-subunit, but not of the beta-subunit
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
preferred substrate, recombinant enzyme
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
best substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
preferred substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
efficient cleavage
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
-
low activity
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
slower cleavage compared to L-Leu-7-amido-4-methylcoumarin
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu 4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
best Xaa-4-nitroanilide substrate
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
best substrate
-
-
?
Leu-4-nitroanilide + H2O
Leu + 4-nitroaniline
-
-
-
?
Leu-Ala-Pro-Tyr-Lys-amide + H2O
Leu + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Leu-Ala-Pro-Tyr-Lys-amide + H2O
Leu + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
low activity
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline
-
low activity
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Met-4-nitroanilide + H2O
Met + 4-nitroaniline
-
-
-
?
Pro-Ala-Pro-Tyr-Lys-amide + H2O
Pro + Ala-Pro-Tyr-Lys-amide
-
best pentapeptide substrate
-
?
Pro-Ala-Pro-Tyr-Lys-amide + H2O
Pro + Ala-Pro-Tyr-Lys-amide
-
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
-
-
-
?
Val-4-nitroanilide + H2O
Val + 4-nitroaniline
low activity
-
?
additional information
?
-
-
non-specific enzyme, broad substrate spectrum, but no hydrolysis of Xaa-Pro bonds
-
?
additional information
?
-
-
no activity with the peptide APGDRIYVHPF, the enzyme does not cleave Xaa-Pro bonds, peptide APGDRIYVHPF as well as proteins casein, soy, and gluten are completely hydrolyzed when the enzyme is accompanied by X-prolyl dipeptidyl aminopeptidase and subtilisin, respectively, overview
-
-
?
additional information
?
-
-
no hydrolyis of N-alpha-benzoyl-DL-Arg 2-naphthylamide
-
-
?
additional information
?
-
-
substrate specificity, no activity with L-Pro-7-amido-4-methylcoumarin and L-Asp-7-amido-4-methylcoumarin, L-Ser-7-amido-4-methylcoumarin is a poor substrate, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with dipeptides D-Phe-D-Phe, Ala-Phe, Asp-Phe, and Pro-Phe, Phe-Gly, Phe-Asp, Phe-Glu, Phe-Val, Phe-Pro, and Phe-Ser, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, no activity with L-Arg-7-amido-4-methylcoumarin and L-Glu-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the alpha-subunits hydrolyzes peptides with neutral N-terminal amino acids while the beta-subunit acts on peptides with acidic N-terminal Glu or Asp residues
-
-
?
additional information
?
-
-
the enzyme prefers peptide substrates with an N-terminal hydrophobic amino acid residue
-
-
?
additional information
?
-
-
ERAP1 trims a large variety of long peptide sequences efficiently, and its activity drops dramatically for peptides shorter than eight or nine amino acids, the enzyme efficiently excises virtually any amino acid in the context of a larger peptide, ERAP1 has broad N-terminal specificity due to strong preferences for residues downstream in the peptide-substrate sequence
-
-
?
additional information
?
-
trimming of the N-terminal leucine residue by ERAP1 is faster for larger peptides of more than 10 residues long
-
-
?
additional information
?
-
-
trimming of the N-terminal leucine residue by ERAP1 is faster for larger peptides of more than 10 residues long
-
-
?
additional information
?
-
-
ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules, overview, loss of enzyme results in disruption of generation of naturally processed peptides in the endoplasmic reticulum, decreased stability of peptide-MHC class I complexes, and diminished CD8+ T cell responses
-
-
?
additional information
?
-
-
ERAP1 trims MHC class I-presented peptides in vivo and plays an important role in immunodominance, overview
-
-
?
additional information
?
-
-
ERAP1 does not degrade other substrates of the X-7-amido-4-methylcoumarin form except L-Leu-7-amido-4-methylcoumarin and L-Met-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
ERAP1 trims peptides with length of 10-14 residues very efficiently down to 8-9 residues long while further trimming is practically absent
-
-
?
additional information
?
-
-
no activity with 4-nitroanilides of Pro, Ile, Val, and Phe
-
?
additional information
?
-
-
no activity with 4-nitroanilides of Pro, Ile, Val, and Phe
-
?
additional information
?
-
-
L-Val-p-nitroanilide, L-Leu-p-nitroanilide, L-Ala-Ala-Ala-p-nitroanilide, N-succinyl-Ala-Ala-Val-p-nitroanilide, N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, benzoyl-Phe-Val-Arg-p-nitroanilide, and benzoyl-Arg-p-nitroanilide are no substrates
-
-
?
additional information
?
-
-
overview, peptidyl substrates, Leu and other hydrophobic amino acids are best substrates, Gly and other charged amino acids are split off more slowly
-
-
?
additional information
?
-
-
no hydrolyis of succinyl-Ala-Ala-Pro-Phe 4-nitroanilide, succinyl-Ala-Ala-Pro-Leu 4-nitroanilide, succinyl-Ala-Ala-Val- Ala 4-nitroanilide, benzyloxycarbonyl-Arg-Arg 4-nitroanilide, benzyloxycarbonyl-Gly-Pro 4-nitroanilide, benzyloxycarbonyl-Pro-Phe-Arg 4-nitroanilide, acetyl-Arg-Gly-Gly-Met 4-nitroanilide, benzoyl-Ile-Glu-Gly-Arg 4-nitroanilide, benzoyl-Tyr 4-nitroanilide, benzyloxycarbonyl-Lys-Arg 4-nitroanilide
-
-
?
additional information
?
-
-
the glycosylated Ape2 aminopeptidase might be responsible for uptake of hydrophobic peptides, especially of leucine N-terminal peptides
-
-
?
additional information
?
-
-
the enzyme cleaves internal peptide binds in di- and tripeptides with preference for hydrophobic N-terminal amino acids
-
-
?
additional information
?
-
-
the enzyme prefers substrates with N-terminal leucine or another hydrophobic amino acid residue, and is less active with Gly or charged amino acids at the P1 position
-
-
?
additional information
?
-
-
the endoplasmic reticulum enzyme ERAP1 trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism, overview, the enzyme is important in antigen presentation, overview
-
-
?
additional information
?
-
-
L-amino acid peptide substrate specificity and strongly preferred chain length of 9-16 residues of isozyme ERAP1, overview, no activity with N-acetylQLESIINFEKL
-
-
?
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1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
inactivation by modification of pK 5.8 carboxylate, presence arginine hydroxamate decreases inhibitory potency, hydroxylamine does not recover enzyme activity
1-Phenyl-2-thiourea
-
competitive
2,3-Dimercaptopropanol
-
-
arginine hydroxamate
-
competitive
chymostatin
-
39% residual activity at 0.1 mM
crystal delta-endotoxin from Bacillus thuringiensis
-
-
-
diethyldicarbonate
-
inactivation by modification of an imidazole, presence of arginine hydroxamate decreases inhibitory potency, hydroxylamine partially recovers enzyme activity after inactivation
dipicolinic acid
97% inhibition at 5 mM, Mg2+, Zn2+, and Co2+ partly protect
Hg2+
-
99% inhibition at 1 mM, recombinant enzyme
Methionine hydroxamate
-
competitive
N-(hydroxyethyl)iminodiacetic acid
-
i.e. Himda
N-p-tosyl-L-lysine chloromethyl ketone
-
64% residual activity at 0.1 mM
N-p-tosyl-L-phenylalanine chloromethyl ketone
-
8% residual activity at 0.1 mM
N-tosyl-L-Phe chloromethyl ketone
-
slightly inhibitory
Nalpha-(2-[[(1-amino-3-phenylpropyl)(hydroxy)phosphoryl]methyl]pent-4-ynoyl)-D-phenylalaninamide
potent phosphinic pseudopeptide inhibitor
Ni2+
-
89% inhibition at 1 mM
nitrobestatin
-
95.1% inhibition at 0.133 mM
p-chloromercuribenzoate
-
-
phebestin
-
i.e. [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl]-L-phenylalanine
Phenylmethylsulfonylfluoride
-
6% residual activity at 1 mM
Tetranitromethane
-
changes the Km of the enzyme without affecting Vmax by modifying a phenol group, presence arginine hydroxamate decreases inhibitory potency
Tris
-
chelated to active site Zn2+
1,10 phenanthroline
-
-
1,10-phenanthroline
-
86.3% inhibition at 5 mM
1,10-phenanthroline
-
87.8% inhibition at 5 mM
1,10-phenanthroline
-
inactivation
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
-
3% residual activity at 10 mM
1,10-phenanthroline
-
half-maximal inhibition at 1.8 mM, competitive and reversible inhibition is reversed by ZnCl2, increases 20fold the inhibition by EDTA
amastatin
-
-
amastatin
-
about 50% inhibition at 0.1 mM
amastatin
-
strong inhibition
amastatin
-
potent inhibitor
amastatin
-
1.5% residual activity at 0.01 mM
bestatin
-
i.e. [(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-valyl]-L-leucine
bestatin
-
92.5% inhibition at 0.3 mM
bestatin
-
87.0% inhibition at 0.3 mM
bestatin
-
strong inhibition
bestatin
-
strong inhibition
bestatin
-
very poor inhibitor
bestatin
-
2% residual activity at 0.01 mM
bestatin
-
strong inhibition
Ca2+
-
16% inhibition at 1 mM, 24% inhibition at 10 mM
Ca2+
-
76% residual activity at 1 mM
Co2+
-
-
Co2+
-
66% inhibition at 0.03 mM
Cu2+
-
noncompetitive
Cu2+
-
complete inhibition at 1 mM, recombinant enzyme
Cu2+
-
32% inhibition at 0.03 mM
DTT
-
25% inhibition at 1 mM, complete inhibition at 10 mM
DTT
-
complete inhibition at 10 mM
EDTA
-
10% inhibition at 1 mM
EDTA
76% inhibition at 10 mM, inhibitory effect is increased by addition of Mg2+, and reversed by addition of Zn2+ and Co2+
EDTA
-
complete inhibition at 1-10 mM
EDTA
-
complete inhibition at 10 mM, Co2+ reactivates, only slight reactivation by Ca2+, Mn2+ and Mg2+, recombinant enzyme
EDTA
-
10 mM, no inhibition at pH 8.1, but conversion into the apoenzyme at pH 6.0
EDTA
-
1.5% residual activity at 5 mM
EDTA
-
inactivation, is affected by pH and temperature, metal binding of at least one deprotonated imidazole group is involved, presence of arginine hydroxamate decreases inhibitory potency, increased by 1,10-phenanthroline
leucinethiol
-
about 80% inhibition at 0.1 mM
Mg2+
-
complete inhibition at 0.03 mM
Mg2+
-
71% residual activity at 1 mM
Mn2+
-
complete inhibition at 10 mM
Mn2+
-
73% inhibition at 1 mM
Mn2+
-
94% inhibition at 0.03 mM
Mn2+
-
complete inhibition at 1 mM
o-phenanthroline
-
91% inhibition at 1 mM
o-phenanthroline
-
96% inhibition
PMSF
-
5% inhibition at 1 mM
PMSF
-
complete inhibition at 10 mM
Urea
-
at 8 M, inhibition of 7% of the enzyme activity with Gly-Leu-Tyr, but 75% of the activity with L-Leu-4-nitroanilide
Zn2+
-
complete inhibition at 0.1-10 mM
Zn2+
-
94% inhibition at 1 mM
Zn2+
-
42% inhibition at 0.03 mM
Zn2+
-
2% residual activity at 1 mM
additional information
-
no inhibition by diisopropyl fluorophosphate, phenylmethylsulfonyl fluoride
-
additional information
-
leuhistin, arphamenine A and B, and actinonin are poor inhibitors
-
additional information
-
no or poor inhibition by Mn2+, Mg2+, and Ca2+
-
additional information
-
no inhibition by epibestatin, and by E64, chymostatin, leupeptin, and antipain
-
additional information
-
no inhibition by epibestatin, and by E64, chymostatin, leupeptin, and antipain
-
additional information
-
not affected by Mg2+
-
additional information
-
no inhibition by DFP
-
additional information
-
no inhibition by EDTA and PMSF
-
additional information
-
not inhibited by pepstatin, L-trans-epoxysuccinyl-leucylamide-(4-guanidino)-butane, alpha1-antitrypsin inhibitor or aprotinin
-
additional information
-
no inhibition by phenylmethylsulfonyl fluoride, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, N.ethylmaleimide, pepstatin, phosphoramidon, puromycin
-
additional information
-
no inhibition by nitriloacetic acid
-
additional information
-
influence of inhibitors on each other, overview, no inhibition by 4-mercuribenzoate, isoamylalcohol and NaF
-
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0.68 - 138
Ala-4-nitroanilide
3.13 - 4.34
Ala-Ala-Pro-Tyr-Lys-amide
0.52
Ala-beta-naphthylamide
-
pH 7.5, 21°C, native enzyme
0.13
Glu-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
0.72 - 6.08
Glu-Ala-Pro-Tyr-Lys-amide
0.88 - 6.08
Gly-Ala-Pro-Tyr-Lys-amide
0.18
Ile-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
0.043 - 0.36
L-Ala-Ala-Pro-Leu-4-nitroanilide
1.43
L-Leu-4-nitroanilide
-
pH 8.5, 65°C
3 - 60
L-leucine 4-nitroanilide
3.8 - 9.5
L-leucine-4-anisidide
6.3 - 16
L-leucine-anilide
0.95
L-Phe-4-nitroanilide
-
pH 8.5, 65°C
0.08
L-Pro-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
0.02
L-Val-4-nitroanilide
-
pH 8.5, 65°C
3.5
Leu-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
3.13 - 3.67
Leu-Ala-Pro-Tyr-Lys-amide
1.8
Lys-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
6.17
Pro-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
7.5 - 12.2
thionoleucine-4-anisidide
7.7 - 23.3
thionoleucine-S-anilide
0.1
Val-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
additional information
Pro-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
0.68
Ala-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
6.08
Ala-4-nitroanilide
-
pH 7.5, 21°C, recombinant enzyme
126.7
Ala-4-nitroanilide
-
pH 7.5, 21°C, native enzyme
138
Ala-4-nitroanilide
-
pH 7.5, 21°C, native enzyme
3.13
Ala-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
4.34
Ala-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
0.72
Glu-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
6.08
Glu-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
0.88
Gly-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
6.08
Gly-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
0.043
L-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 7.2, -1°C
0.13
L-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 7.2, 9°C
0.36
L-Ala-Ala-Pro-Leu-4-nitroanilide
-
pH 7.2, 19°C
3
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
5.3
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
60
L-leucine 4-nitroanilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
3.8
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
9.3
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
9.5
L-leucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
6.3
L-leucine-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
15.1
L-leucine-anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
16
L-leucine-anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
3.13
Leu-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
3.67
Leu-Ala-Pro-Tyr-Lys-amide
-
pH 7.5, 21°C, recombinant enzyme
7.5
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
7.9
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
11.1
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
12.2
thionoleucine-4-anisidide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
7.7
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound
10.6
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Cd2+ bound
11.5
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with 2 Zn2+ bound
16.9
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
23.3
thionoleucine-S-anilide
-
pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound
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Klionsky, D.J.
Nonclassical protein sorting to the yeast vacuole
J. Biol. Chem.
273
10807-10810
1998
Saccharomyces cerevisiae
brenda
Martinez, E.; Jimenez, M.A.; Segui-Real, B.; Vandekerckhove, J.; Sandoval, I.V.
Folding of the presequence of yeast pAPI into an amphipathic helix determines transport of the protein from the cytosol to the vacuole
J. Mol. Biol.
267
1124-1138
1997
Saccharomyces cerevisiae
brenda
Kim, J.; Scott, S.V.; Oda, M.N.; Klionsky, D.J.
Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway
J. Cell Biol.
137
609-618
1997
Saccharomyces cerevisiae
brenda
Scott, S.V.; Baba, M.; Ohsumi, Y.; Klionsky, D.J.
Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism
J. Cell Biol.
138
37-44
1997
Saccharomyces cerevisiae
brenda
Oda, M.N.; Scott, S.V.; Hefner-Gravink, A.; Caffarelli, A.C.; Klionsky, D.J.
Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I
J. Cell Biol.
132
999-1010
1996
Saccharomyces cerevisiae
brenda
Scott, S.V.; Klionsky, D.J.
In vitro reconstitution of cytoplasm to vacuole protein targeting in yeast
J. Cell Biol.
3131
1727-1735
1995
Saccharomyces cerevisiae
brenda
Segui-Real, B.; Martinez, M.; Sandoval, I.V.
Yeast aminopeptidase I is post-translationally sorted from the cytosol to the vacuole by a mechanism mediated by its bipartite N-terminal extension
EMBO J.
14
5476-5484
1995
Saccharomyces cerevisiae
brenda
Tisljar, U.; Wolf, D.H.
Purification and characterization of the cystinyl bond cleaving yeast aminopeptidase yscXVI
FEBS Lett.
322
191-196
1993
Saccharomyces cerevisiae
brenda
Moriyasu, Y.; Sakano, K.; Tazawa, M.
Vacuolar/extravacuolar distribution of aminopeptidase in giant alga Chara australis and partial purification of one such enzyme
Plant Physiol.
84
720-725
1987
Chara australis
brenda
Hetz, G.; Rhm, K.H.
Interaction of chloride with yeast aminopeptidase I. Equilibrium binding studies
Biol. Chem. Hoppe-Seyler
368
63-66
1987
Saccharomyces cerevisiae
brenda
Rhm., K.H.
Chloride as allosteric effector of yeast aminopeptidase I
Arch. Biochem. Biophys.
239
216-225
1985
Saccharomyces cerevisiae
brenda
Rhm., K.H.
Metal binding to yeast aminopeptidase I
Eur. J. Biochem.
146
633-639
1985
Saccharomyces cerevisiae
brenda
Schwencke, J.; Moustacchi, E.
Proteolytic activities in yeast after UV irradiation. I. Variation in proteinase levels in repair proficient Rad+ strains
Mol. Gen. Genet.
185
290-295
1982
Saccharomyces cerevisiae
brenda
Lffler, H.G.; Rhm.K.H.
Comparative studies on the dodecameric and hexameric forms of yeast aminopeptidase I
Z. Naturforsch. C
34
381-386
1979
Saccharomyces cerevisiae
-
brenda
Metz, G.; Marx, R.; Rhm, K.H.
The quarternary structure of yeast aminopeptidase I 1. Molecular forms and subunit size
Z. Naturforsch. C
32
929-937
1977
Saccharomyces cerevisiae
brenda
Metz, G.; Rhm.K.H.
Yeast aminopeptidase I. Chemical composition and catalytic properties
Biochim. Biophys. Acta
429
933-949
1976
Saccharomyces cerevisiae
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