Information on EC 3.4.24.B29 - Sulfolobus solfataricus metalloendopeptidase

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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus

EC NUMBER
COMMENTARY hide
3.4.24.B29
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Sulfolobus solfataricus metalloendopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins, such as azocasein
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
azocasein + H2O
fragments of azocasein
show the reaction diagram
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
5 mM, stimulates activity up to 160%, contains a zinc-binding motif
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
10 mM, 90% inhibition
Co2+
5 mM, 91% inhibition
Cu2+
5 mM, 37% inhibition
E-64
0.01 mM, 44% inhibition
EDTA
5 mM, complete inhibition
Fe2+
5 mM, 93% inhibition
Hg2+
5 mM, 15% inhibition
Mg2+
5 mM, 97% inhibition
Mn2+
5 mM, 37% inhibition
N-ethylmaleimide
5 mM, 64% inhibition
Sr2+
5 mM, 83% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
leupeptin
1 mM, 1.7fold activation
PMSF
5 mM, 1.2fold activation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
6: more than 75% of maximal activity, pH 9: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 85
45°C: about 85% of maximal activity, 85°C: about 60% of maximal activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
2 * 55000, the protein forms disulfide bond via the Cys416 residue, yielding protein dimer that is the active form of the enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 55000, the protein forms disulfide bond via the Cys416 residue, yielding protein dimer that is the active form of the enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C416G
4% of the activity compared to wild-type enzyme, azocasein as substrate
E229D
11% of the activity compared to wild-type enzyme, azocasein as substrate
H228F
8% of the activity compared to wild-type enzyme, azocasein as substrate
H233Y
14% of the activity compared to wild-type enzyme, azocasein as substrate