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).^[1]^[2]^[3]^[4]^[5] 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. and Hightower, L.E. (1992). "Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange". Biochemistry 31: 9406–9412. doi:10.1021/bi00154a012. PMID 1356434.
↑ Blond-Elquindi, S., Fourie, A.M., Sambrook, J.F. and Gething, M.J. (1993). "Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers". J. Biol. Chem. 268: 12730–12735. PMID 8509407.
↑ Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C. and Zylicz, M. (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". EMBO J. 14: 1867–1877. PMID 7743994.
↑ Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R. and Joachimiak, A. (1997). "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain". Structure 5: 403–414. doi:10.1016/s0969-2126(97)00197-4. PMID 9083109.
↑ Li, X., Su, R.T., Hsu, H.T. and Sze, H. (1998). "The molecular chaperone calnexin associated with the vacuolar H⁺-ATPase from oat seedlings". Plant Cell 10: 119–130. doi:10.2307/3870633. PMID 9477575.

External links

Non-chaperonin molecular chaperone ATPase at the US 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_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2

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 Tubulin

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

Non-chaperonin molecular chaperone ATPase

See also

References

External links