3.6.4.B10: chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)

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Word Map on EC 3.6.4.B10

3.6.4.B10

chaperonins

tubulins

actin

hetero-oligomeric

cytoskeletal

groel

prefoldin

chaperonin-containing

huntingtin

proteostasis

double-ring

tailless

polyglutamine

polyq

inter-ring

phosducin-like

synthesis

back-to-back

drug development

protein-folding

homo-oligomeric

acidophilum

beta-tubulin

thermoplasma

medicine

cryo-electron

Reaction

Synonyms

alpha/beta-thermosome, ApCpnB, archaeal chaperonin, CCT, CCT ATPase, CCT chaperonin, CCT complex, CCT/TRiC, CCT/TRiC chaperonin, CCT/TRiC complex, CCT2, chaperonin B, chaperonin containing t-complex polypeptide-1, chaperonin containing TCP-1, chaperonin containing TCP1, chaperonin TCP-1 ring complex, chaperonin TRiC, chaperonin TRiC/CCT, chaperonin-containing t-complex polypeptide 1, cPKA, CpkB, CtCCT, cytosolic chaperonin TRiC, eukaryotic chaperone complex, eukaryotic chaperonin, eukaryotic chaperonin TRiC, eukaryotic group II chaperonin, GaTRiC, group II chaperonin, group II chaperonin CCT/TRiC, group II CPN, HsTRiC, Mm-cpn, MmCpn, More, PfCPN, PfTRiC, PhCPN, Plasmodium TRiC, protein P45, T-complex polypeptide-1 ring complex, T-complex protein 1, T-complex protein 1 ring complex, T-complex protein-1 ring complex, TCP-1, TCP-1 ring complex, TCP1, TCP1 ring complex, thermosome, TKS1-CPN, TriC, TRiC chaperonin, TRiC chaperonin complex, TRiC/CCT, type II chaperonin

ECTree

3 Hydrolases

3.6 Acting on acid anhydrides

3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement

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

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Results	in table
3	Activating Compound
12	AA Sequence
7	Application
21	Cloned(Commentary)
13	Cofactor
9	Crystallization (Commentary)
242	Disease/ Diagnostics
8	Expression
184	General Information
1	General Stability
2	Inhibitors
14	KM Value [mM]
40	Localization
52	Metals/Ions
16	Molecular Weight [Da]
67	Natural Substrates/ Products (Substrates)
106	Organism
15	pH Optimum
2	Posttranslational Modification
74	Protein Variants
19	Purification (Commentary)
2	Reaction
86	Reference
1	Renatured (Commentary)
34	Source Tissue
105	Substrates and Products (Substrate)
43	Subunits
224	Synonyms
18	Temperature Optimum [°C]
4	Temperature Range [°C]
1	Temperature Stability [°C]

Temperature Optimum

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

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Saccharomyces cerevisiae

P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079

assay at

751330

Mus musculus

P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932

assay at

757660

Thermochaetoides thermophila

assay at

758147

3 entries

Glaciozyma antarctica

A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7

refolding/ATPase

756410

Thermococcus kodakarensis

P61111, Q52500

mutants Q533G and E530G

734095

2 entries

60 - 70

Thermococcus kodakarensis

P61111, Q52500

wild-type enzyme and mutant P538G

734095

Thermococcus kodakarensis

P61111, Q52500

mutants P533M, D545M, and E530M

734095

3 entries

Pyrococcus horikoshii

O57762

assay at

744559

Pyrococcus horikoshii

O57762

724949