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Information on EC 3.6.4.B10 - chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

for references in articles please use BRENDA:EC3.6.4.B10
preliminary BRENDA-supplied EC number
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UNIPROT: O57762
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
Synonyms
tcp-1, t-complex protein 1, cct complex, tric/cct, chaperonin containing tcp-1, eukaryotic chaperonin, cct/tric, cct chaperonin, chaperonin tric/cct, chaperonin tric, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group II chaperonin
Pyrococcus species contain only one chaperonin gene per whole genome
PhCPN
additional information
ordered locus name: PH0017
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
with the addition of Mg2+ ion protection activity on inorganic phosphatase from thermal inactivation at 85°C and 110°C increases 2fold compared with the addition of enzyme alone
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
prefoldin
the enzyme is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 95
70°C: about 70% of maximal activity, 95°C: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THS_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
549
0
59693
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59600, SDS-PAGE
hexadecamer
homooligomer, double-ring structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the recombinant enzyme is purified to 91% by heat-shock treatment and anion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
the chaperonin gene PhCpn is amplified by PCR from the genomic DNA, subcloned into pET21a vector, and expressed in three Escherichia coli host cells such as BL21, Rosetta, and Codonplus (DE3)DE3. Among these host cells, Escherichia coli Rosetta shows the highest expression level of recombinant PhCpn at induction with 1 mM isopropyl beta-D-thiogalactoside
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okochi, M.; Matsuzaki, H.; Nomura, T.; Ishii, N.; Yohda, M.
Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
Extremophiles
9
127-134
2004
Pyrococcus horikoshii (O57762), Pyrococcus horikoshii OT-3 (O57762)
Manually annotated by BRENDA team
Kim, J.; Shin, E.; Jeon, S.; Kim, Y.; Kim, P.; Lee, C.; Nam, S.
Overexpression, purification, and functional characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
Biotechnol. Bioprocess Eng.
14
551-558
2009
Pyrococcus horikoshii (O57762)
-
Manually annotated by BRENDA team