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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.24.B29 - Sulfolobus solfataricus metalloendopeptidase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q7LXP6

for references in articles please use BRENDA:EC3.4.24.B29
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
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q7LXP6
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
hydrolysis of proteins, such as azocasein
Synonyms
sso0660, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
5 mM, stimulates activity up to 160%, contains a zinc-binding motif
INHIBITOR
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
SUBUNIT
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
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hu, Y.; Peng, N.; Han, W.; Mei, Y.; Chen, Z.; Feng, X.; Liang, Y.X.; She, Q.
An archaeal protein evolutionarily conserved in prokaryotes is a zinc-dependent metalloprotease
Biosci. Rep.
32
609-618
2012
Saccharolobus solfataricus (Q7LXP6), Saccharolobus solfataricus
Manually annotated by BRENDA team