3.4.11.B5: Thermococcus onnurineus deblocking aminopeptidase
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For detailed information about Thermococcus onnurineus deblocking aminopeptidase, go to the full flat file.
Reaction
Catalytic efficiency for hydrolysis of N-leucyl 4-nitroanilide is 105fold higher than catalytic efficiency for hydrolysis of N-acetyl-L-leucyl 4-nitroanilide. Catalytic efficiency for hydrolysis of L-methionyl 4-nitroanilide is similar to 5fold higher compared to catalytic efficiency for hydrolysis of l-leucyl 4-nitroanilide =
Synonyms
deblocking aminopeptidase, TNA1-DAP, TNA1-DAP1, TNA1-DAP2, TNA1-DAP3, TNA1-DAP4
ECTree
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Metals Ions
Metals Ions on EC 3.4.11.B5 - Thermococcus onnurineus deblocking aminopeptidase
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Ba2+
Co2+
Cu2+
Mg2+
Mn2+
Ni2+
additional information
Ba2+
activates, relative activity is about 90% compared to Mn2+
-
0.5 mM Co2+ stimulates activity 4.8fold, the enzyme contains 0.09 mol of Co2+ per mol of monomer
Co2+
activates, relative activity is about 80% compared to Mn2+, 0.1 mM Co2+ in assay mixture
relative activity is about 30% compared to Mn2+
Cu2+
relative activity is about 35% compared to Mg2+
Mg2+
activates, relative activity is about 80% compared to Mn2+
Mn2+
relative activity is about 75% compared to Mg2+
relative activity is about 40% compared to Mn2+
Ni2+
relative activity is about 80% compared to Mg2+
-
metal binding residues are His71, Asp188, Asp 244, and Glu222
additional information
metal binding residues are His71, Asp188, Asp 244, and Glu222
additional information
metal binding residues are His71, Asp188, Asp 244, and Glu222
additional information
metal binding residues are His71, Asp188, Asp 244, and Glu222