Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.11.B3 - Sulfolobus solfataricus aminopeptidase and Organism(s) Saccharolobus solfataricus and UniProt Accession P95928

for references in articles please use BRENDA:EC3.4.11.B3
preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.B3 Sulfolobus solfataricus aminopeptidase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharolobus solfataricus
UNIPROT: P95928
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Saccharolobus solfataricus
Reaction Schemes
hide
Preferentially hydrolyzes Xaa-/-Yaa-, in which Xaa is preferentially a non-polar amino acid, L-Ala or L-Leu. When Xaa is L-Phe or a polar amino acid residue like L-Gly or a basic amino acid residue like L-Lys and L-Arg the rates of hydrolysis are lower
Synonyms
intracellular Sulfolobus aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intracellular Sulfolobus aminopeptidase
-
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanyl 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
show the reaction diagram
about 70% of the activity compared to L-leucyl 4-nitroanilide
-
-
?
L-arginyl 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
show the reaction diagram
about 30% of the activity compared to L-leucyl 4-nitroanilide
-
-
?
L-leucyl 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-lysyl 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
about 15% of the activity compared to L-leucyl 4-nitroanilide
-
-
?
L-methionyl 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
show the reaction diagram
about 70% of the activity compared to L-leucyl 4-nitroanilide
-
-
?
L-phenylalanyl 4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
show the reaction diagram
about 35% of the activity compared to L-leucyl 4-nitroanilide
-
-
?
L-prolyl 4-nitroanilide + H2O
L-proline + 4-nitroaniline
show the reaction diagram
about 20% of the activity compared to L-leucyl 4-nitroanilide
-
-
?
glycyl 4-nitroanilide + H2O
glycine + 4-nitroaniline
show the reaction diagram
-
11% of the activity compared to L-Leu-4-nitroanilide
-
-
?
L-alanyl 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
show the reaction diagram
-
118% of the activity compared to L-Leu-4-nitroanilide
-
-
?
L-arginyl 4-nitroanilide + H2O
L-arginine + 4-nitroaniline
show the reaction diagram
-
63% of the activity compared to L-Leu-4-nitroanilide
-
-
?
L-leucyl 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-lysyl 4-nitroanilide + H2O
L-lysine + 4-nitroaniline
show the reaction diagram
-
15% of the activity compared to L-Leu-4-nitroanilide
-
-
?
L-phenylalanyl 4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
show the reaction diagram
-
62% of the activity compared to L-Leu-4-nitroanilide
-
-
?
additional information
?
-
-
no activity with N-acetyl-L-phenylalanine, N-acetyl-L-leucine, N-benzoyl-L-arginine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
zinc-dependent enzyme
Co2+
-
1 mM, restores enzyme activity after inhibition with EDTA
Mn2+
-
1 mM, restores enzyme activity after inhibition with EDTA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
1 mM, complete inhibition
acetic acid
-
1%, 86% inhibition
acetonitrile
-
10%, 26% inhibition
bestatin
-
1 mM, 97% inhibition
EDTA
-
1 mM, complete inhibition
ethanol
-
10%, complete inhibition
mercaptoethanol
-
1%, 56% inhibition
SDS
-
0.1%, complete inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21
L-alanyl 4-nitroanilide
-
pH 7.0, 70°C
0.1
L-leucyl 4-nitroanilide
-
pH 7.0, 70°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.225
-
pH 7.0, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
pH 5.5: about 45% of maximal activity, pH 7.5: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
adition of 0.05 mM each of Co2+, Mn2+, Mg2+, Ca2+ and Zn2+ has no effect on the temperature optimum. At higher concentrations of divalent metal ions a decrease of activity occurs
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 95
80°C: optimum, 95°C: 40% of maximal activity, no activity below 30°C
60 - 90
-
60°C: about 60% of maximal activity, 90°C: about 35% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
x * 90000, SDS-PAGE
320000
-
gel filtration
80000
-
4 * 80000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 90000, SDS-PAGE
homotetramer
-
4 * 80000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
14 h, at least 70% residual activity
718953
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
15 min, activity decreases to 10% in absence of Co2+, in presence of 0.05 mM the remaining activity is 76%
85
-
15 min, complete loss of activity in absence of Co2+, in presence of 0.05 mM the remaining activity is 60%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Condo, I.; Ruggero, D.; Reinhardt, R.; Londei, P.
A novel aminopeptidase associated with the 60 kDa chaperonin in the thermophilic archaeon Sulfolobus solfataricus
Mol. Microbiol.
29
775-785
1998
Saccharolobus solfataricus (P95928)
Manually annotated by BRENDA team
Hanner, M.; Redl, B.; Stffler, G.
Isolation and characterization of an intracellular aminopeptidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus
Biochim. Biophys. Acta
1033
148-153
1990
Saccharolobus solfataricus
Manually annotated by BRENDA team