List of optimization software: Difference between revisions

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{{Infobox enzyme
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| Name = Non-chaperonin molecular chaperone ATPase
| EC_number = 3.6.4.10
| CAS_number =
| IUBMB_EC_number = 3/6/4/10
| GO_code =
| image =
| width =
| caption =
}}
'''Non-chaperonin molecular chaperone ATPase''' ({{EC number|3.6.4.10}}, ''molecular chaperone Hsc70 ATPase'') is an [[enzyme]] with system name ''ATP phosphohydrolase (polypeptide-polymerizing)''.<ref>{{cite journal | title = Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange |author = Sadis, S. and Hightower, L.E. |journal = Biochemistry |year = 1992 |volume = 31 |pages = 9406–9412 |pmid = 1356434}}</ref><ref>{{cite journal | title = Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers |author = Blond-Elquindi, S., Fourie, A.M., Sambrook, J.F. and Gething, M.J. |journal = J. Biol. Chem. |year = 1993 |volume = 268 |pages = 12730–12735 |pmid = 8509407}}</ref><ref>{{cite journal | title = The ClpX heat-shock protein of ''Escherichia coli'', the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone |author = Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C. and Zylicz, M. |journal = EMBO J. |year = 1995 |volume = 14 |pages = 1867–1877 |pmid = 7743994}}</ref><ref>{{cite journal | title = Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain |author = Sriram, M., Osipiuk, J., Freeman, B., Morimoto, R. and Joachimiak, A. |journal = Structure |year = 1997 |volume = 5 |pages = 403–414 |pmid = 9083109}}</ref><ref>{{cite journal | title = The molecular chaperone calnexin associated with the vacuolar H<sup>+</sup>-ATPase from oat seedlings |author = Li, X., Su, R.T., Hsu, H.T. and Sze, H. |journal = Plant Cell |year = 1998 |volume = 10 |pages = 119–130 |pmid = 9477575}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]
 
: ATP + H<sub>2</sub>O <math>\rightleftharpoons</math> ADP + [[phosphate]]
 
These enzymes perform many functions that are similar to those of [[chaperonin]]s.
 
== See also ==
* [[Chaperone (protein)]]
 
== References ==
{{reflist}}
 
== External links ==
* {{MeshName|Non-chaperonin+molecular+chaperone+ATPase}}
 
[[Category:EC 3.6.4]]

Latest revision as of 13:31, 7 January 2015

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