Non-chaperonin molecular chaperone ATPase

Class of enzymes

Non-chaperonin molecular chaperone ATPase

Identifiers
EC no.| 3.6.4.10
Databases
IntEnz| IntEnz view
BRENDA| BRENDA entry
ExPASy| NiceZyme view
KEGG| KEGG entry
MetaCyc| metabolic pathway
PRIAM| profile
PDB structures| RCSB PDB PDBe PDBsum
| Search

PMC| articles
PubMed| articles
NCBI| proteins

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  ⇌ {\displaystyle \rightleftharpoons } ADP + phosphate

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

## See also

[edit]

* Chaperone (protein)

## References

[edit]

1. ^ 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 1356434.9406-12&rft.date=1992-10&rft_id=info:doi/10.1021/bi00154a012&rft_id=info:pmid/1356434&rft.aulast=Sadis&rft.aufirst=S&rft.au=Hightower,+LE&rfr_id=info:sid/en.wikipedia.org:Non-chaperonin+molecular+chaperone+ATPase" class="Z3988">
2. ^ 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 8509407.12730-5&rft.date=1993-06&rft_id=info:pmid/8509407&rft.aulast=Blond-Elguindi&rft.aufirst=S&rft.au=Fourie,+AM&rft.au=Sambrook,+JF&rft.au=Gething,+MJ&rfr_id=info:sid/en.wikipedia.org:Non-chaperonin+molecular+chaperone+ATPase" class="Z3988">
3. ^ 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 7743994.1867-77&rft.date=1995-05&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398286#id-name=PMC&rft_id=info:pmid/7743994&rft.aulast=Wawrzynow&rft.aufirst=A&rft.au=Wojtkowiak,+D&rft.au=Marszalek,+J&rft.au=Banecki,+B&rft.au=Jonsen,+M&rft.au=Graves,+B&rft.au=Georgopoulos,+C&rft.au=Zylicz,+M&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC398286&rfr_id=info:sid/en.wikipedia.org:Non-chaperonin+molecular+chaperone+ATPase" class="Z3988">
4. ^ 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 9083109.403-14&rft.date=1997-03&rft_id=info:doi/10.1016/s0969-2126(97)00197-4&rft_id=info:pmid/9083109&rft.aulast=Sriram&rft.aufirst=M&rft.au=Osipiuk,+J&rft.au=Freeman,+B&rft.au=Morimoto,+R&rft.au=Joachimiak,+A&rft_id=https://doi.org/10.1016%2Fs0969-2126%2897%2900197-4&rfr_id=info:sid/en.wikipedia.org:Non-chaperonin+molecular+chaperone+ATPase" class="Z3988">
5. ^ 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 9477575.119-30&rft.date=1998-01&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC143936#id-name=PMC&rft_id=info:pmid/9477575&rft_id=info:doi/10.2307/3870633&rft.aulast=Li&rft.aufirst=X&rft.au=Su,+RT&rft.au=Hsu,+HT&rft.au=Sze,+H&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC143936&rfr_id=info:sid/en.wikipedia.org:Non-chaperonin+molecular+chaperone+ATPase" class="Z3988">

## External links

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

* v
* t
* e

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1|

* Pyrophosphatase
* Inorganic
* Thiamine
* Apyrase
* Thiamine-triphosphatase

3.6.2|

* Adenylylsulfatase
* Phosphoadenylylsulfatase

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|

* Dynein
* Kinesin
* Myosin
* Katanin

3.6.5: GTPase|

| 3.6.5.1: Heterotrimeric G protein|

* Gαs
* Golf
* Gαi
* GNAI1
* GNAI2
* GNAI3
* Transducin
* GNAT1
* GNAT2
* Gustducin
* GNAT3
* Gαq/11
* GNAQ
* GNA11
* Gα12/13
* 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

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* 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

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