Information on EC 3.4.11.16 - Xaa-Trp aminopeptidase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.4.11.16
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RECOMMENDED NAME
GeneOntology No.
Xaa-Trp aminopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
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exopeptidase, N-terminus, amino acid
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CAS REGISTRY NUMBER
COMMENTARY hide
137010-33-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Trp + H2O
Ala + Trp
show the reaction diagram
-
-
-
ir
alpha-Asp-Phe + H2O
Asp + Phe
show the reaction diagram
alpha-Asp-Phe-Met + H2O
Asp + Phe-Met
show the reaction diagram
alpha-Asp-Phe-NH2 + H2O
Asp + Phe-NH2
show the reaction diagram
Arg-Trp + H2O
Arg + Trp
show the reaction diagram
-
-
-
ir
Asp-Phe + H2O
Asp + Phe
show the reaction diagram
-
-
-
ir
Asp-Phe-NH2 + H2O
Asp + Phe-NH2
show the reaction diagram
-
-
-
-
?
Glu-Trp + H2O
Glu + Trp
show the reaction diagram
Glu-Tyr + H2O
Glu + Tyr
show the reaction diagram
-
-
-
ir
Gly-Trp + H2O
Gly + Trp
show the reaction diagram
Gly-Tyr + H2O
Gly + Tyr
show the reaction diagram
-
-
-
ir
Ile-Phe + H2O
Ile + Phe
show the reaction diagram
-
-
-
ir
Ile-Trp + H2O
Ile + Trp
show the reaction diagram
-
-
-
ir
Leu-enkephalin + H2O
Leu + enkephalin
show the reaction diagram
-
low activity
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ir
Leu-Phe + H2O
Leu + Phe
show the reaction diagram
-
-
-
ir
Leu-Trp + H2O
Leu + Trp
show the reaction diagram
Leu-Trp-Leu + H2O
Leu + Trp-Leu
show the reaction diagram
Leu-Trp-Met-Arg + H2O
Leu + Trp-Met-Arg
show the reaction diagram
Leu-Tyr + H2O
Leu + Tyr
show the reaction diagram
-
-
-
ir
Peptides + H2O
?
show the reaction diagram
Phe-Phe + H2O
Phe + Phe
show the reaction diagram
-
-
-
ir
Phe-Trp + H2O
Phe + Trp
show the reaction diagram
-
-
-
ir
Phe-Tyr + H2O
Phe + Tyr
show the reaction diagram
-
-
-
ir
Pro-Trp + H2O
Pro + Trp
show the reaction diagram
-
-
-
ir
Trp-Phe + H2O
Trp + Phe
show the reaction diagram
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-
-
ir
Trp-Trp + H2O
Trp + Trp
show the reaction diagram
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-
-
ir
Tyr-Leu + H2O
Tyr + Leu
show the reaction diagram
-
-
-
ir
Tyr-Phe + H2O
Tyr + Phe
show the reaction diagram
-
-
-
ir
Val-Trp + H2O
Val + Trp
show the reaction diagram
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-
-
ir
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Peptides + H2O
?
show the reaction diagram
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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50% inhibition at 0.6 mM
amastatin
Arphamenine A
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50% inhibition at 0.1 mM
Arphamenine B
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7% inhibition at 0.1 mM
bestatin
captopril
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
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phosphate
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probestin
rentiapril
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
zofenoprilat
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.625
Ala-Trp
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3.11
alpha-Asp-Phe
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-
7.48
alpha-Asp-Phe-NH2
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4.96
Aspartame
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0.568
Glu-Trp
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1.757
Gly-Trp
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0.488
Leu-Trp
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1.7
Pro-Trp
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38.5
Ala-Trp
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117
alpha-Asp-Phe
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230
alpha-Asp-Phe-NH2
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238
Aspartame
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113
Glu-Trp
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127
Gly-Trp
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92.6
Leu-Trp
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29.6
Pro-Trp
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13 - 16
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substrate-dependent
68050
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additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
7.5
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substrate Leu-Trp
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
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substrate Leu-Trp
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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expressed both in undifferentiated and differentiated cell lines
Manually annotated by BRENDA team
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myelinated and unmyelinated neurons of the peripheral nervous system
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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cells expressing the enzyme intracellularly do not necessarily express it at the surface
Manually annotated by BRENDA team
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cells expressing the enzyme intracellularly do not necessarily express it at the surface
Manually annotated by BRENDA team
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integral membrane protein, microvillar membrane
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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dimer, ultrastructural study, uncertain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.11.16)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)