BRENDA - Enzyme Database
show all sequences of 3.5.1.57

Tryptophanyl aminopeptidase

Adachi, O.; Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press 1, 1014-1015 (2004)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
enzymatic method of L-tryptophan production. The enzyme is useful for the manufacturing process because it is not inhibited by high levels of product
Cutaneotrichosporon cutaneum
Inhibitors
Inhibitors
Commentary
Organism
Structure
2,2'-dipyridyl
-
Cutaneotrichosporon cutaneum
additional information
no inhibition by high levels of the product L-tryptophan
Cutaneotrichosporon cutaneum
NEM
-
Cutaneotrichosporon cutaneum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Cutaneotrichosporon cutaneum
5829
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
25% of the activation with Mn2+
Cutaneotrichosporon cutaneum
Mn2+
2.5 mM required for full activity
Cutaneotrichosporon cutaneum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
68000
-
4 * 68000, SDS-PAGE
Cutaneotrichosporon cutaneum
270000
-
gel filtration
Cutaneotrichosporon cutaneum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cutaneotrichosporon cutaneum
-
IFO 0173
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-alaninamide + H2O
hydrolyzed 14% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-alanine + NH3
-
-
-
?
L-asparagine + H2O
hydrolyzed 22% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-aspartate + NH3
-
-
-
?
L-citrulline + H2O
hydrolyzed 22% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
?
-
-
-
?
L-glutamine + H2O
hydrolyzed 18% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-glutamate + NH3
-
-
-
?
L-leucinamide + H2O
hydrolyzed 26% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-leucine + NH3
-
-
-
?
L-methioninamide + H2O
hydrolyzed 14% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-methionine + NH3
-
-
-
?
L-phenylalaninamide + H2O
hydrolyzed 47% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-phenylalanine + NH3
-
-
-
?
L-serinamide + H2O
hydrolyzed 7% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-serine + NH3
-
-
-
?
L-tryptophanamide + H2O
-
668755
Cutaneotrichosporon cutaneum
L-tryptophan + NH3
-
-
-
?
L-tyrosinamide + H2O
hydrolyzed 22% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-tyrosine + NH3
-
-
-
?
L-valinamide + H2O
hydrolyzed 15% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-valine + NH3
-
-
-
?
additional information
high affinity towards peptides having a L-Trp residue at the N-terminal moiety
668755
Cutaneotrichosporon cutaneum
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 68000, SDS-PAGE
Cutaneotrichosporon cutaneum
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
45
-
Cutaneotrichosporon cutaneum
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
55
-
10 min, stable
Cutaneotrichosporon cutaneum
60
-
rapid inactivation
Cutaneotrichosporon cutaneum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
9.5
-
Cutaneotrichosporon cutaneum
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7.5
8.5
room temperature, 20 h, no appreciable loss of activity
Cutaneotrichosporon cutaneum
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Cutaneotrichosporon cutaneum
isoelectrofocusing
-
4.7
Application (protein specific)
Application
Commentary
Organism
synthesis
enzymatic method of L-tryptophan production. The enzyme is useful for the manufacturing process because it is not inhibited by high levels of product
Cutaneotrichosporon cutaneum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2,2'-dipyridyl
-
Cutaneotrichosporon cutaneum
additional information
no inhibition by high levels of the product L-tryptophan
Cutaneotrichosporon cutaneum
NEM
-
Cutaneotrichosporon cutaneum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Cutaneotrichosporon cutaneum
5829
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
25% of the activation with Mn2+
Cutaneotrichosporon cutaneum
Mn2+
2.5 mM required for full activity
Cutaneotrichosporon cutaneum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
68000
-
4 * 68000, SDS-PAGE
Cutaneotrichosporon cutaneum
270000
-
gel filtration
Cutaneotrichosporon cutaneum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-alaninamide + H2O
hydrolyzed 14% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-alanine + NH3
-
-
-
?
L-asparagine + H2O
hydrolyzed 22% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-aspartate + NH3
-
-
-
?
L-citrulline + H2O
hydrolyzed 22% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
?
-
-
-
?
L-glutamine + H2O
hydrolyzed 18% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-glutamate + NH3
-
-
-
?
L-leucinamide + H2O
hydrolyzed 26% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-leucine + NH3
-
-
-
?
L-methioninamide + H2O
hydrolyzed 14% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-methionine + NH3
-
-
-
?
L-phenylalaninamide + H2O
hydrolyzed 47% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-phenylalanine + NH3
-
-
-
?
L-serinamide + H2O
hydrolyzed 7% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-serine + NH3
-
-
-
?
L-tryptophanamide + H2O
-
668755
Cutaneotrichosporon cutaneum
L-tryptophan + NH3
-
-
-
?
L-tyrosinamide + H2O
hydrolyzed 22% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-tyrosine + NH3
-
-
-
?
L-valinamide + H2O
hydrolyzed 15% as rapidly as L-tryptophanamide
668755
Cutaneotrichosporon cutaneum
L-valine + NH3
-
-
-
?
additional information
high affinity towards peptides having a L-Trp residue at the N-terminal moiety
668755
Cutaneotrichosporon cutaneum
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 68000, SDS-PAGE
Cutaneotrichosporon cutaneum
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
40
45
-
Cutaneotrichosporon cutaneum
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
55
-
10 min, stable
Cutaneotrichosporon cutaneum
60
-
rapid inactivation
Cutaneotrichosporon cutaneum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
9
9.5
-
Cutaneotrichosporon cutaneum
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7.5
8.5
room temperature, 20 h, no appreciable loss of activity
Cutaneotrichosporon cutaneum
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Cutaneotrichosporon cutaneum
isoelectrofocusing
-
4.7
Other publictions for EC 3.5.1.57
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
668755
Adachi
-
Tryptophanyl aminopeptidase ...
Cutaneotrichosporon cutaneum
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
1014-1015
2004
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1
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3
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2
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1
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12
1
1
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2
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1
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1
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1
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1
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-
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3
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1
2
2
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12
1
1
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2
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1
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1
1
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209203
Murphy
-
Localization and characterizat ...
Arabidopsis sp.
Plant Physiol. Biochem.
37
431-443
1999
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1
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1
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4
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4
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81203
Iwayama
-
Crystallization and characteri ...
Cutaneotrichosporon cutaneum
Agric. Biol. Chem.
47
2483-2493
1983
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11
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6
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1
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1
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1
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1
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11
1
1
1
2
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1
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1
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