Information on EC 3.4.11.B6 - Thermococcus kodakarensis deblocking aminopeptidase

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The expected taxonomic range for this enzyme is: Thermococcus kodakarensis

EC NUMBER
COMMENTARY hide
3.4.11.B6
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Thermococcus kodakarensis deblocking aminopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
TkDAP1 prefers to degrade unblocked, polar substrate (L-leucyl 4-nitroanilide) and blocked non-polar peptide (N-acetyl-Ala-Ala-Ala). TkDAP2 has high activity towards both unblocked substrates (L-leucyl 4-nitroanilide and Ala-Ala-Ala), irrespective of polarity.
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala-Ala 4-nitroanilide + H2O
L-alanine + Ala-Ala-Ala 4-nitroanilide
show the reaction diagram
about 10% of the activity with L-leucyl 4-nitroanilide
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?
Ala-Ala-Ala-4-nitroanilide + H2O
L-alanine + Ala-Ala-Ala 4-nitroanilide
show the reaction diagram
about 10% of the activity with Leu-4-nitroanilide
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?
L-leucyl 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
highest specific activity compared to other substrates tested
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?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-L-alanine + Ala-Ala
show the reaction diagram
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
show the reaction diagram
about 30% of the activity with L-leucyl 4-nitroanilide
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
substrate: Ala-Ala-Ala 4-nitroanilide; substrate: N-acetyl-Ala-Ala-Ala
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
substrate: Ala-Ala-Ala 4-nitroanilide; substrate: N-acetyl-Ala-Ala-Ala
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 100
60C: about 40% of maximal activity, 100C: about 70% of maximal activity; 60C: about 60% of maximal activity, 100C: about 70% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
trimer, gel filtration
450000
octadecamer, gel filtration; octadecamer, gel filtration
670000
dodecamer, gel filtration
690000
dodecamer, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
the enzyme displays an octadecamer and dodecamer assembly. The dodecameric structure is the main one; the enzyme displays a trimer, octadecamer and dodecamer assembly. The dodecamer structure is the main one
octadecamer
the enzyme displays an octadecamer and dodecamer assembly. The dodecameric structure is the main one; the enzyme displays a trimer, octadecamer and dodecamer assembly. The dodecamer structure is the main one
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by heat and oxidative stress; induced by heat and oxidative stress
not induced by heat and oxidative stress; not induced by heat and oxidative stress