Literature summary for 3.4.11.B6 extracted from

Jia, B.; Lee, S.; Pham, B.P.; Kwack, J.M.; Jin, H.; Li, J.; Wang, Y.; Cheong, G.W.
Biochemical characterization of deblocking aminopeptidases from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (2011), Biosci. Biotechnol. Biochem., 75, 1160-1166.

Search for more literature for 3.4.11.B6

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermococcus kodakarensis

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	-	Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
120000	-	trimer, gel filtration	Thermococcus kodakarensis
450000	-	octadecamer, gel filtration	Thermococcus kodakarensis
670000	-	dodecamer, gel filtration	Thermococcus kodakarensis
690000	-	dodecamer, gel filtration	Thermococcus kodakarensis

Organism

Organism	UniProt	Comment	Textmining
Thermococcus kodakarensis	Q5JH87	-	-
Thermococcus kodakarensis	Q5JHA5	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Ala-Ala-Ala 4-nitroanilide + H2O	about 10% of the activity with L-leucyl 4-nitroanilide	Thermococcus kodakarensis	L-alanine + Ala-Ala-Ala 4-nitroanilide	-	?
Ala-Ala-Ala-4-nitroanilide + H2O	about 10% of the activity with Leu-4-nitroanilide	Thermococcus kodakarensis	L-alanine + Ala-Ala-Ala 4-nitroanilide	-	?
L-leucyl 4-nitroanilide + H2O	highest specific activity compared to other substrates tested	Thermococcus kodakarensis	L-leucine + 4-nitroaniline	-	?
N-acetyl-Ala-Ala-Ala + H2O	about 65% of the activity with L-leucyl 4-nitroanilide	Thermococcus kodakarensis	N-acetyl-L-alanine + Ala-Ala	-	?
N-acetyl-Ala-Ala-Ala + H2O	about 65% of the activity with Leu-4-nitroanilide	Thermococcus kodakarensis	N-acetyl-L-alanine + Ala-Ala	-	?
N-acetyl-L-leucyl 4-nitroanilide + H2O	about 30% of the activity with L-leucyl 4-nitroanilide	Thermococcus kodakarensis	N-acetyl-L-leucine + 4-nitroaniline	-	?

Subunits

Subunits	Comment	Organism
dodecamer	the enzyme displays a trimer, octadecamer and dodecamer assembly. The dodecamer structure is the main one	Thermococcus kodakarensis
dodecamer	the enzyme displays an octadecamer and dodecamer assembly. The dodecameric structure is the main one	Thermococcus kodakarensis
octadecamer	the enzyme displays a trimer, octadecamer and dodecamer assembly. The dodecamer structure is the main one	Thermococcus kodakarensis
octadecamer	the enzyme displays an octadecamer and dodecamer assembly. The dodecameric structure is the main one	Thermococcus kodakarensis

Synonyms

Synonyms	Comment	Organism
deblocking aminopeptidase	ambiguous	Thermococcus kodakarensis
TK0775	-	Thermococcus kodakarensis
TK0781	-	Thermococcus kodakarensis
TkDAP1	-	Thermococcus kodakarensis
TkDAP2	-	Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
80	-	substrate: Ala-Ala-Ala 4-nitroanilide	Thermococcus kodakarensis
80	-	substrate: N-acetyl-Ala-Ala-Ala	Thermococcus kodakarensis

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
60	100	60°C: about 40% of maximal activity, 100°C: about 70% of maximal activity	Thermococcus kodakarensis
60	100	60°C: about 60% of maximal activity, 100°C: about 70% of maximal activity	Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	substrate: Ala-Ala-Ala 4-nitroanilide	Thermococcus kodakarensis
7.4	-	substrate: N-acetyl-Ala-Ala-Ala	Thermococcus kodakarensis

pH Range

pH Minimum	pH Maximum	Comment	Organism
6.2	8	pH 6.2: about 35% of maximal activity, pH 8.0: about 50% of maximal activity, substrate: Ala-Ala-Ala 4-nitroanilide	Thermococcus kodakarensis
6.2	8.5	pH 6.2: about 50% of maximal activity, pH 8.5: about 50% of maximal activity, substrate: N-acetyl-Ala-Ala-Ala	Thermococcus kodakarensis

Expression

Organism	Comment	Expression
Thermococcus kodakarensis	not induced by heat and oxidative stress	additional information
Thermococcus kodakarensis	induced by heat and oxidative stress	up

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Release 2023.1 (January 2023)