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Literature summary extracted from

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

Application

EC Number Application Comment Organism
3.5.1.57 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

EC Number Inhibitors Comment Organism Structure
3.5.1.57 2,2'-dipyridyl
-
Cutaneotrichosporon cutaneum
3.5.1.57 additional information no inhibition by high levels of the product L-tryptophan Cutaneotrichosporon cutaneum
3.5.1.57 NEM
-
Cutaneotrichosporon cutaneum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.57 cytosol
-
Cutaneotrichosporon cutaneum 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.57 Co2+ 25% of the activation with Mn2+ Cutaneotrichosporon cutaneum
3.5.1.57 Mn2+ 2.5 mM required for full activity Cutaneotrichosporon cutaneum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.57 68000
-
4 * 68000, SDS-PAGE Cutaneotrichosporon cutaneum
3.5.1.57 270000
-
gel filtration Cutaneotrichosporon cutaneum

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.57 Cutaneotrichosporon cutaneum
-
IFO 0173
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.57 L-alaninamide + H2O hydrolyzed 14% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-alanine + NH3
-
?
3.5.1.57 L-asparagine + H2O hydrolyzed 22% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-aspartate + NH3
-
?
3.5.1.57 L-citrulline + H2O hydrolyzed 22% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum ?
-
?
3.5.1.57 L-glutamine + H2O hydrolyzed 18% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-glutamate + NH3
-
?
3.5.1.57 L-leucinamide + H2O hydrolyzed 26% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-leucine + NH3
-
?
3.5.1.57 L-methioninamide + H2O hydrolyzed 14% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-methionine + NH3
-
?
3.5.1.57 L-phenylalaninamide + H2O hydrolyzed 47% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-phenylalanine + NH3
-
?
3.5.1.57 L-serinamide + H2O hydrolyzed 7% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-serine + NH3
-
?
3.5.1.57 L-tryptophanamide + H2O
-
Cutaneotrichosporon cutaneum L-tryptophan + NH3
-
?
3.5.1.57 L-tyrosinamide + H2O hydrolyzed 22% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-tyrosine + NH3
-
?
3.5.1.57 L-valinamide + H2O hydrolyzed 15% as rapidly as L-tryptophanamide Cutaneotrichosporon cutaneum L-valine + NH3
-
?
3.5.1.57 additional information high affinity towards peptides having a L-Trp residue at the N-terminal moiety Cutaneotrichosporon cutaneum ?
-
?

Subunits

EC Number Subunits Comment Organism
3.5.1.57 tetramer 4 * 68000, SDS-PAGE Cutaneotrichosporon cutaneum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.57 40 45
-
Cutaneotrichosporon cutaneum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.57 55
-
10 min, stable Cutaneotrichosporon cutaneum
3.5.1.57 60
-
rapid inactivation Cutaneotrichosporon cutaneum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.57 9 9.5
-
Cutaneotrichosporon cutaneum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.57 7.5 8.5 room temperature, 20 h, no appreciable loss of activity Cutaneotrichosporon cutaneum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.5.1.57 Cutaneotrichosporon cutaneum isoelectrofocusing
-
4.7