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IUBMB CommentsRequires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.
The enzyme appears in viruses and cellular organisms
Synonyms
aminopeptidase, tryptophan, L-tryptophan aminopeptidase, tryptophan aminopeptidase,
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aminopeptidase, tryptophan
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L-tryptophan aminopeptidase
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tryptophan aminopeptidase
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L-tryptophanamide + H2O = L-tryptophan + NH3
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hydrolysis of linear amides
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L-tryptophanamide amidohydrolase
Requires Mn2+. Also acts on N-ethylformamide and L-tyrosinamide, and on some tryptophan dipeptides.
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glycine-beta-naphthylamide + H2O
glycine + 2-naphthylamine
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L-alaninamide + H2O
L-alanine + NH3
L-asparagine + H2O
L-aspartate + NH3
L-citrullin + H2O
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22% of the activity with L-tryptophanamide
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L-citrulline + H2O
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hydrolyzed 22% as rapidly as L-tryptophanamide
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L-glutamine + H2O
L-glutamate + NH3
L-leucinamide + H2O
L-leucine + NH3
L-methioninamide + H2O
L-methionine + NH3
L-phenylalaninamide + H2O
L-phenylalanine + NH3
L-proline-beta-naphthylamide + H2O
L-proline + 2-naphthylamine
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L-serinamide + H2O
L-serine + NH3
L-tryptophan-beta-naphthylamide + H2O
L-tryptophan + 2-naphthylamine
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L-tryptophanamide + H2O
L-tryptophan + NH3
L-tyrosinamide + H2O
L-tyrosine + NH3
L-tyrosine-beta-naphthylamide + H2O
L-Tyr + 2-naphthylamine
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L-valinamide + H2O
L-valine + NH3
additional information
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high affinity towards peptides having a L-Trp residue at the N-terminal moiety
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L-alaninamide + H2O
L-alanine + NH3
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14% of the activity with L-tryptophanamide
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L-alaninamide + H2O
L-alanine + NH3
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hydrolyzed 14% as rapidly as L-tryptophanamide
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L-asparagine + H2O
L-aspartate + NH3
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22% of the activity with L-tryptophanamide
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L-asparagine + H2O
L-aspartate + NH3
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hydrolyzed 22% as rapidly as L-tryptophanamide
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L-glutamine + H2O
L-glutamate + NH3
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18% of the activity with L-tryptophanamide
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L-glutamine + H2O
L-glutamate + NH3
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hydrolyzed 18% as rapidly as L-tryptophanamide
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L-leucinamide + H2O
L-leucine + NH3
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26% of the activity with L-tryptophanamide
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L-leucinamide + H2O
L-leucine + NH3
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hydrolyzed 26% as rapidly as L-tryptophanamide
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L-methioninamide + H2O
L-methionine + NH3
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14% of the activity with L-tryptophanamide
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L-methioninamide + H2O
L-methionine + NH3
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hydrolyzed 14% as rapidly as L-tryptophanamide
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L-phenylalaninamide + H2O
L-phenylalanine + NH3
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47% of the activity with L-tryptophanamide
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L-phenylalaninamide + H2O
L-phenylalanine + NH3
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hydrolyzed 47% as rapidly as L-tryptophanamide
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L-serinamide + H2O
L-serine + NH3
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7% of the activity with L-tryptophanamide
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L-serinamide + H2O
L-serine + NH3
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hydrolyzed 7% as rapidly as L-tryptophanamide
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L-tryptophanamide + H2O
L-tryptophan + NH3
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L-tryptophanamide + H2O
L-tryptophan + NH3
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L-tyrosinamide + H2O
L-tyrosine + NH3
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22% of the activity with L-tryptophanamide
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L-tyrosinamide + H2O
L-tyrosine + NH3
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hydrolyzed 22% as rapidly as L-tryptophanamide
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L-valinamide + H2O
L-valine + NH3
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15% of the activity with L-tryptophanamide
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L-valinamide + H2O
L-valine + NH3
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hydrolyzed 15% as rapidly as L-tryptophanamide
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L-tryptophanamide + H2O
L-tryptophan + NH3
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Co2+
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25% of the activation with Mn2+
Mn2+
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required for activity
Mn2+
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2.5 mM required for full activity
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1,10-phenanthroline
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weak
additional information
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no inhibition by high levels of the product L-tryptophan
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5.6
L-Tryptophanamide
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9 - 9.5
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9 - 9.5
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crystalline enzyme
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40 - 45
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40 - 45
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crystalline enzyme
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35 - 60
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crystalline enzyme, 35°C: about 75% of activity maximum, 60°C: about 35% of activity maximum
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brenda
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brenda
IFO 0173
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brenda
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hypocotyl transition zone
brenda
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brenda
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brenda
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68000
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4 * 68000, SDS-PAGE
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tetramer
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4 * 68000, SDS-PAGE
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7.5 - 8.5
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crystalline enzyme, pH 7.5, 20 h, room temperature
81203
7.5 - 8.5
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room temperature, 20 h, no appreciable loss of activity
668755
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55
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10 min, stable
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crystalline enzyme, 10 min, stable
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rapid inactivation
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crystalline enzyme, rapid inactivation
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synthesis
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enzymatic method of L-tryptophan production. The enzyme is useful for the manufacturing process because it is not inhibited by high levels of product
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Iwayama, A.; Kimura, T.; Adachi, O.; Ameyama, M.
Crystallization and characterization of a novel aminopeptidase from Trichosporon cutaneum
Agric. Biol. Chem.
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2483-2493
1983
Cutaneotrichosporon cutaneum
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brenda
Murphy, A.; Taiz, L.
Localization and characterization of soluble and plasma membrane aminopeptidase activities in Arabidopsis seedlings
Plant Physiol. Biochem.
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431-443
1999
Arabidopsis sp.
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brenda
Adachi, O.
Tryptophanyl aminopeptidase
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
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1014-1015
2004
Cutaneotrichosporon cutaneum
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brenda
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