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Information on EC 3.4.11.6 - aminopeptidase B and Organism(s) Bacillus subtilis and UniProt Accession P25152

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.6 aminopeptidase B
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This record set is specific for:
Bacillus subtilis
UNIPROT: P25152 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Synonyms
apb, arylamidase, aminopeptidase b, arginine aminopeptidase, cytosol aminopeptidase, arginyl aminopeptidase, aminopeptidase-b, dap bii, l-rap, arginine-aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
double-zinc aminopeptidase
-
aminopeptidase, arginine
-
-
-
-
arginine aminopeptidase
-
-
-
-
arginyl aminopeptidase
-
-
-
-
arylamidase II
-
-
-
-
Cl--activated arginine aminopeptidase
-
-
-
-
cytosol aminopeptidase
-
-
-
-
L-arginine aminopeptidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9073-92-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Ala-4-nitroanilide + H2O
L-Ala + 4-nitroaniline
show the reaction diagram
low activity
-
-
?
L-Arg-4-nitroanilide + H2O
L-Arg + 4-nitroaniline
show the reaction diagram
best substrate
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Lys-4-nitroanilide + H2O
L-Lys + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Val-4-nitroanilide + H2O
L-Val + 4-nitroaniline
show the reaction diagram
low activity
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc-metalloaminopeptidase, 2 Zn2+ per enzyme molecule
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
complete inhibition, reversible by Zn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10
L-Ala-4-nitroanilide
pH 8.0, 30°C
0.6
L-Arg-4-nitroanilide
pH 8.0, 30°C
3.6
L-Leu-4-nitroanilide
pH 8.0, 30°C
0.85
L-Lys-4-nitroanilide
pH 8.0, 30°C
19
L-Val-4-nitroanilide
pH 8.0, 30°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37
L-Ala-4-nitroanilide
pH 8.0, 30°C
34
L-Arg-4-nitroanilide
pH 8.0, 30°C
55
L-Leu-4-nitroanilide
pH 8.0, 30°C
10
L-Lys-4-nitroanilide
pH 8.0, 30°C
0.43
L-Val-4-nitroanilide
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ywad gene
SwissProt
Manually annotated by BRENDA team
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
20 min, purified recombinant enzyme, stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 5fold from Escherichia coli by ion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ywad, overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fundoiano-Hershcovitz, Y.; Rabinovitch, L.; Shulami, S.; Reiland, V.; Shoham, G.; Shoham, Y.
The ywad gene from Bacillus subtilis encodes a double-zinc aminopeptidase
FEMS Microbiol. Lett.
243
157-163
2005
Bacillus subtilis (P25152), Bacillus subtilis
Manually annotated by BRENDA team