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EC Tree
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on Glu-/-Trp, Leu-/-Trp and a number of other dipeptides
Synonyms
aminopeptidase W, aminopeptidase X-Trp,
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aminopeptidase X-Trp
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Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on Glu-/-Trp, Leu-/-Trp and a number of other dipeptides
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hydrolysis of peptide bond
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exopeptidase, N-terminus, amino acid
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Ala-Trp + H2O
Ala + Trp
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ir
alpha-Asp-Phe + H2O
Asp + Phe
alpha-Asp-Phe-Met + H2O
Asp + Phe-Met
alpha-Asp-Phe-NH2 + H2O
Asp + Phe-NH2
Arg-Trp + H2O
Arg + Trp
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-
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ir
Asp-Phe + H2O
Asp + Phe
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-
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ir
Asp-Phe-NH2 + H2O
Asp + Phe-NH2
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?
aspartame + H2O
?
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-
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?
Glu-Tyr + H2O
Glu + Tyr
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-
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ir
Gly-Tyr + H2O
Gly + Tyr
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-
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ir
Ile-Phe + H2O
Ile + Phe
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-
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ir
Ile-Trp + H2O
Ile + Trp
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-
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ir
Leu-enkephalin + H2O
Leu + enkephalin
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low activity
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ir
Leu-Phe + H2O
Leu + Phe
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-
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ir
Leu-Trp-Leu + H2O
Leu + Trp-Leu
Leu-Trp-Met-Arg + H2O
Leu + Trp-Met-Arg
Leu-Tyr + H2O
Leu + Tyr
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-
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ir
Phe-Phe + H2O
Phe + Phe
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-
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ir
Phe-Trp + H2O
Phe + Trp
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-
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ir
Phe-Tyr + H2O
Phe + Tyr
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-
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ir
Pro-Trp + H2O
Pro + Trp
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-
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ir
Trp-Phe + H2O
Trp + Phe
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-
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ir
Trp-Trp + H2O
Trp + Trp
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-
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ir
Tyr-Leu + H2O
Tyr + Leu
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-
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ir
Tyr-Phe + H2O
Tyr + Phe
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-
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ir
Val-Trp + H2O
Val + Trp
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ir
additional information
?
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alpha-Asp-Phe + H2O
Asp + Phe
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ir
alpha-Asp-Phe + H2O
Asp + Phe
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ir
alpha-Asp-Phe-Met + H2O
Asp + Phe-Met
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ir
alpha-Asp-Phe-Met + H2O
Asp + Phe-Met
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ir
alpha-Asp-Phe-NH2 + H2O
Asp + Phe-NH2
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ir
alpha-Asp-Phe-NH2 + H2O
Asp + Phe-NH2
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ir
Glu-Trp + H2O
Glu + Trp
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ir
Glu-Trp + H2O
Glu + Trp
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?
Glu-Trp + H2O
Glu + Trp
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ir
Glu-Trp + H2O
Glu + Trp
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ir
Gly-Trp + H2O
Gly + Trp
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-
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ir
Gly-Trp + H2O
Gly + Trp
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-
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ir
Leu-Trp + H2O
Leu + Trp
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-
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ir
Leu-Trp + H2O
Leu + Trp
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ir
Leu-Trp + H2O
Leu + Trp
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ir
Leu-Trp-Leu + H2O
Leu + Trp-Leu
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-
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ir
Leu-Trp-Leu + H2O
Leu + Trp-Leu
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-
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ir
Leu-Trp-Met-Arg + H2O
Leu + Trp-Met-Arg
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ir
Leu-Trp-Met-Arg + H2O
Leu + Trp-Met-Arg
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ir
Peptides + H2O
?
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time course of activity during cell growth and proliferation
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ir
Peptides + H2O
?
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involved in intestinal breakdown and uptake of aspartame
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ir
Peptides + H2O
?
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ir
Peptides + H2O
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involved in intestinal digestion of small, pre-digested peptide fragments
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ir
additional information
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may be involved in neuropeptide metabolism, may play a minor role in the intestinal metabolism of the artificial sweetener aspartame
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?
additional information
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the enzyme cleaves Leu-/-Trp, it prefers short peptides with an aromatic residue in the P1' position, with Glu-/-Trp being the best substrate. Dipeptides with Trp, Phe or Tr in the P1' position are rapidly hydrolyzed. The requirement in the P1 position is no stringent. Te enzyme does not hydrolyze N-blocked peptides
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?
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additional information
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may be involved in neuropeptide metabolism, may play a minor role in the intestinal metabolism of the artificial sweetener aspartame
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?
Peptides + H2O
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time course of activity during cell growth and proliferation
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ir
Peptides + H2O
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involved in intestinal breakdown and uptake of aspartame
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ir
Peptides + H2O
?
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ir
Peptides + H2O
?
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involved in intestinal digestion of small, pre-digested peptide fragments
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ir
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Zn
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the enzyme contains 1.2 atoms of zinc per subunit
Zn2+
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1.2 mol zinc per mol enzyme, probably involved in catalysis
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2-mercaptoethanol
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50% inhibition at 0.6 mM
Arphamenine A
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50% inhibition at 0.1 mM
Arphamenine B
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7% inhibition at 0.1 mM
cilazaprilat
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27% inhibition at 0.1 mM
Co2+
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65-90% inhibition at 1 mM
Cu2+
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65-90% inhibition at 1 mM
dithiothreitol
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50% inhibition at 0.1 mM
lisinopril
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28% inhibition at 0.1 mM
Ni2+
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25% inhibition at 1 mM
pentoprilat
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27% inhibition at 0.1 mM
spiraprilat
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28% inhibition at 0.1 mM
Zn2+
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65-90% inhibition at 1 mM, reactivated at 10 mM EDTA
amastatin
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50% inhibition at 0.002 mM
amastatin
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100% inhibition at 0.1 mM
amastatin
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50% inhibition at 0.00158 mM
bestatin
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some of the observed chemotherapeutic actions of bestatin may be due to inhibition of enzyme
bestatin
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50% inhibition at 0.006 mM
bestatin
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89% inhibition at 0.1 mM
bestatin
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50% inhibition at 0.0079 mM
captopril
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50% inhibition at 0.3 mM
captopril
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56% inhibition at 0.1 mM
probestin
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% inhibition at 0.1 mM
probestin
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50% inhibition at 0.005 mM
rentiapril
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100% inhibition at 0.1 mM
rentiapril
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50% inhibition at 0.0016 mM
rentiapril
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the enzyme has an overlapping substrate specificity and inhibitor profile with the related mammalian membrane-bound zinc aminopeptidases membrane alanyl aminopeptidase (EC 3.4.11.2) and glutamyl aminopeptidase (EC 3.4.11.16), but can be distinguished from them by its inhibition by rentiopril and zofenoprilat
zofenoprilat
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82% inhibition at 0.1 mM
zofenoprilat
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50% inhibition at 0.018 mM
zofenoprilat
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the enzyme has an overlapping substrate specificity and inhibitor profile with the related mammalian membrane-bound zinc aminopeptidases membrane alanyl aminopeptidase (EC 3.4.11.2) and glutamyl aminopeptidase (EC 3.4.11.16), but can be distinguished from them by its inhibition by rentiopril and zofenoprilat
additional information
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many group-specific inhibitors for cysteine proteases have no effect
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additional information
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overlap of inhibitory effects of typical aminopeptidase inhibitors with other enzymes
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7.48
alpha-Asp-Phe-NH2
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230
alpha-Asp-Phe-NH2
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13 - 16
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substrate-dependent
additional information
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time course of activity during cell growth and proliferation
additional information
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activity highly buffer-dependent, optimal in 100 mM Tris-HCl
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7
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assay at
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6 - 10
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substrate Leu-Trp
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37
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assay at
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brenda
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brenda
antibody studies
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brenda
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expressed both in undifferentiated and differentiated cell lines
brenda
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myelinated and unmyelinated neurons of the peripheral nervous system
brenda
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brenda
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brenda
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expressed both in undifferentiated and differentiated cell lines
brenda
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brenda
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brenda
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4% of activity of renal cortex
brenda
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no activity
brenda
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162% of activity of renal cortex
brenda
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brenda
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brenda
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75% of activity of human duodenal mucosa
brenda
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brenda
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72% of activity of renal cortex
brenda
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brenda
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renal cortex
brenda
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proximal tubule
brenda
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cells expressing the enzyme intracellularly do not necessarily express it at the surface
brenda
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cells expressing the enzyme intracellularly do not necessarily express it at the surface
brenda
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integral membrane protein, microvillar membrane
brenda
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brenda
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brenda
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reconstituted into microvillar liposomes
brenda
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130000
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additional information
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dimer, ultrastructural study, uncertain
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glycoprotein
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glycoprotein
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31% carbohydrates
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medicine
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chemotherapeutic target, involved in heart disease, metastasis, inflammation
medicine
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model system for enterocytic differentiation, but caution necessary because of inhomogenities concerning enzyme expression within cell lines
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Gee, N.S.; Kenny, A.J.
Proteins of the kidney microvillar membrane. Enzymic and molecular properties of aminopeptidase W
Biochem. J.
246
97-102
1987
Sus scrofa
brenda
Gee, N.S.; Kenny, A.J.
Aminopeptidase W: a new brush-border hydrolase identified by a monoclonal antibody
Biochem. Soc. Trans.
14
76-77
1986
Sus scrofa
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brenda
Gee, N.S.; Kenny, A.J.
Proteins of the kidney microvillar membrane. The 130 kDa protein in pig kidney, recognized by monoclonal antibody GK5C1, is an ectoenzyme with aminopeptidase activity
Biochem. J.
230
753-764
1985
Sus scrofa
brenda
Howell, S.; Brewis, I.A.; Hooper, N.M.; Kenny, A.J.; Turner, A.J.
Mosaic expression of membrane peptidases by confluent cultures of Caco-2 cells
FEBS Lett.
317
109-112
1993
Homo sapiens
brenda
Howell, S.; Kenny, A.J.; Turner, J.
A survey of membrane peptidases in two human colonic cell lines, Caco-2 and HTZ-29
Biochem. J.
284
595-601
1992
Homo sapiens
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brenda
Tieku, S.; Hooper, M.
Inhibition of aminopeptidases N, A, and W
Biochem. Pharmacol.
44
1725-1730
1992
Homo sapiens, Sus scrofa
brenda
Tieku, S.; Hooper, N.M.
Inhibitor profile of porcine aminopeptidase W
Biochem. Soc. Trans.
21
250S
1993
Homo sapiens, Sus scrofa
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brenda
Hooper, N.M.; Hesp, R.J.; Tieku, S.
Metabolism of aspartame by human and pig intestinal microvillar peptidases
Biochem. J.
298
635-639
1994
Homo sapiens, Sus scrofa
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brenda
Hooper, N.M.
X-Trp aminopeptidase
Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)
2nd. ed.
1013-1014
2004
Sus scrofa
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brenda
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3.4.11.16 Xaa-Trp aminopeptidase
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