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Information on EC 3.4.11.16 - Xaa-Trp aminopeptidase
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3.4.11.16 Xaa-Trp aminopeptidaseSpecify your search results
Word Map
- 3.4.11.16
- peptidases
- endopeptidase-24.11
- dipeptidase
- microvillar
-
dipeptidyl
- carboxypeptidase
-
cell-surface
-
ileum
- aminopeptidases
- bestatin
-
hydrolysed
- medicine
- amastatin
-
brush
-
choroid
-
3.4.11.7
-
microvessels
- endopeptidase-2
-
neuropeptide
-
brush-border
- angiotensin
-
immunoperoxidase
- 1,10-phenanthroline
-
caco-2
-
histochemistry
- jejunum
- actinonin
-
plexus
-
immunoradiometric
-
3.4.24.11
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ectoenzyme
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase X-Trp
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, amino acid
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CAS REGISTRY NUMBER
COMMENTARY
137010-33-4
-
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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
Peptides + H2O
?
-
time course of activity during cell growth and proliferation
-
-
ir
Peptides + H2O
?
-
involved in intestinal breakdown and uptake of aspartame
-
-
ir
Peptides + H2O
?
-
involved in intestinal digestion of small, pre-digested peptide fragments
-
-
ir
additional information
?
-
-
may be involved in neuropeptide metabolism, may play a minor role in the intestinal metabolism of the artificial sweetener aspartame
-
-
?
additional information
?
-
-
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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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
additional information
?
-
-
may be involved in neuropeptide metabolism, may play a minor role in the intestinal metabolism of the artificial sweetener aspartame
-
-
?
Peptides + H2O
?
-
time course of activity during cell growth and proliferation
-
-
ir
Peptides + H2O
?
-
involved in intestinal breakdown and uptake of aspartame
-
-
ir
Peptides + H2O
?
-
involved in intestinal digestion of small, pre-digested peptide fragments
-
-
ir
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bestatin
-
some of the observed chemotherapeutic actions of bestatin may be due to inhibition of enzyme
rentiapril
-
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
-
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
-
many group-specific inhibitors for cysteine proteases have no effect
-
additional information
-
overlap of inhibitory effects of typical aminopeptidase inhibitors with other enzymes
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
time course of activity during cell growth and proliferation
additional information
-
activity highly buffer-dependent, optimal in 100 mM Tris-HCl
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expressed both in undifferentiated and differentiated cell lines
brenda
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myelinated and unmyelinated neurons of the peripheral nervous system
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expressed both in undifferentiated and differentiated cell lines
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cells expressing the enzyme intracellularly do not necessarily express it at the surface
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cells expressing the enzyme intracellularly do not necessarily express it at the surface
brenda
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
chemotherapeutic target, involved in heart disease, metastasis, inflammation
medicine
-
model system for enterocytic differentiation, but caution necessary because of inhomogenities concerning enzyme expression within cell lines
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
-
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
-
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
-
brenda
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