Literature summary for 3.4.11.B4 extracted from

Onoe, S.; Ando, S.; Ataka, M.; Ishikawa, K.
Active site of deblocking aminopeptidase from Pyrococcus horikoshii (2002), Biochem. Biophys. Res. Commun., 290, 994-997.

Search for more literature for 3.4.11.B4

Cloned(Commentary)

Cloned (Comment)	Organism
-	Pyrococcus horikoshii

Protein Variants

Protein Variants	Comment	Organism
D173N	Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced	Pyrococcus horikoshii
E205Q	Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced	Pyrococcus horikoshii
E206Q	Km-value for Ala-Ala-Ala is not significantly different from the KM-value for the wild-type enzyme, kcat is significantly reduced	Pyrococcus horikoshii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
3.4	-	Ala-Ala-Ala	pH 7.5, 85°C, mutant enzyme D173N, medium containing 8 mM Co2+	Pyrococcus horikoshii
4.8	-	Ala-Ala-Ala	pH 7.5, 85°C, wild-type enzyme, medium containing 2 mM Co2+	Pyrococcus horikoshii
7.4	-	Ala-Ala-Ala	pH 7.5, 85°C, mutant enzyme E206Q, medium containing 8 mM Co2+	Pyrococcus horikoshii
8.7	-	Ala-Ala-Ala	pH 7.5, 85°C, mutant enzyme E205Q, medium containing 8 mM Co2+	Pyrococcus horikoshii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	contains 1.32 mol of Ca2+ per mol of monomer	Pyrococcus horikoshii
Co2+	wild-type enzyme is strongly activated by Co2+. Activity of mutant enzymes D173N, E205Q, and E206Q is slightly increased by Co2+. Asp173, Glu205, and Glu206 participate in the catalytic activity through binding with the Co2+	Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
36900	-	x * 36900, wild-type enzyme, mutant enzymes D173N, E205Q and E206Q, SDS-PAGE	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O58255	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Ala-Ala-Ala + H2O	-	Pyrococcus horikoshii	Ala-Ala + L-alanine	-	?

Subunits

Subunits	Comment	Organism
?	x * 36900, wild-type enzyme, mutant enzymes D173N, E205Q and E206Q, SDS-PAGE	Pyrococcus horikoshii

Synonyms

Synonyms	Comment	Organism
DAPPh	-	Pyrococcus horikoshii
deblocking aminopeptidase	-	Pyrococcus horikoshii
PH0519	-	Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
85	-	assay at	Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.091	-	Ala-Ala-Ala	pH 7.5, 85°C, mutant enzyme D173N, medium containing 8 mM Co2+	Pyrococcus horikoshii
0.093	-	Ala-Ala-Ala	pH 7.5, 85°C, mutant enzyme E205Q, medium containing 8 mM Co2+	Pyrococcus horikoshii
0.226	-	Ala-Ala-Ala	pH 7.5, 85°C, mutant enzyme E206Q, medium containing 8 mM Co2+	Pyrococcus horikoshii
2.08	-	Ala-Ala-Ala	pH 7.5, 85°C, wild-type enzyme, medium without Co2+	Pyrococcus horikoshii
9.01	-	Ala-Ala-Ala	pH 7.5, 85°C, wild-type enzyme, medium containing 2 mM Co2+	Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Pyrococcus horikoshii

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Release 2023.1 (January 2023)