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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.4.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
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:
UNIPROT: Q9YDK6
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
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
-
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
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
?
UTP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
thermal protection assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha-subunit ApCpnA; gene thsA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
chaperonins are ubiquitous chaperones that are required for correct protein folding, assembly, and degradation
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THSA_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
554
0
60374
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60700
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE
61200
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant alpha-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene thsA, recombinant expression of alpha-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, J.W.; Kim, S.W.; Kim, J.H.; Jeon, S.J.; Kwon, H.J.; Kim, B.W.; Nam, S.W.
Functional characterization of the alpha- and beta-subunits of a group II chaperonin from Aeropyrum pernix K1
J. Microbiol. Biotechnol.
23
818-825
2013
Aeropyrum pernix (Q9YA66), Aeropyrum pernix (Q9YDK6), Aeropyrum pernix (Q9YDK6 and Q9YA66), Aeropyrum pernix DSM 11879 (Q9YDK6 and Q9YA66)
Manually annotated by BRENDA team