Non-chaperonin molecular chaperone ATPase

Non-chaperonin molecular chaperone ATPase (EC 3.6.4.10, molecular chaperone Hsc70 ATPase) is an enzyme with systematic name ATP phosphohydrolase (polypeptide-polymerizing). This enzyme catalyses the following chemical reaction

ATP + H₂O

\rightleftharpoons

ADP + phosphate

These enzymes perform many functions that are similar to those of chaperonins.

References

Sadis S, Hightower LE (October 1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry. 31 (39): 9406–12. doi:10.1021/bi00154a012. PMID 1356434.
Blond-Elguindi S, Fourie AM, Sambrook JF, Gething MJ (June 1993). "Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers". The Journal of Biological Chemistry. 268 (17): 12730–5. PMID 8509407.
Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M (May 1995). "The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone". The EMBO Journal. 14 (9): 1867–77. PMC 398286. PMID 7743994.
Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A (March 1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure. 5 (3): 403–14. doi:10.1016/s0969-2126(97)00197-4. PMID 9083109.
Li X, Su RT, Hsu HT, Sze H (January 1998). "The molecular chaperone calnexin associates with the vacuolar H(+)-ATPase from oat seedlings". The Plant Cell. 10 (1): 119–30. doi:10.2307/3870633. PMC 143936. PMID 9477575.

External links

Non-chaperonin+molecular+chaperone+ATPase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B
Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2
Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4
H+/K+ (3.6.3.10)	ATP4A
Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_olf G_αi GNAI1 GNAI2 GNAI3 Transducin GNAT1 GNAT2 Gustducin GNAT3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13
3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK
3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic
3.6.5.5-6: Polymerization motors	dynamin superfamily Dynamin Guanylate-binding protein Mitofusin-1 MX1 and MX2 OPA1 Tubulin

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.6.4

Misplaced Pages

Non-chaperonin molecular chaperone ATPase

See also

References

External links