Biology:Mitochondrial protein-transporting ATPase
| mitochondrial protein-transporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.3.51 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a mitochondrial protein-transporting ATPase (EC 3.6.3.51) is an enzyme that catalyzes the chemical reaction
- ATP + H2O [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are ADP and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides to catalyse transmembrane movement of substances. The systematic name of this enzyme class is ATP phosphohydrolase (mitochondrial protein-importing). During the interactions of the proteins Hsp70 and sunbit Tim44, ATPase domain is essential.[1] Without the presence of ATPase, carboxy-terminal segment is not able to bind to protein of Tim44.[1] As mtHsp70 transmits the nucleotide state of the ATPase domain with alpha-helices A and B, Tim44 interacts with the peptide binding domain to coordinate the protein bind.[2]
References
- ↑ 1.0 1.1 Krimmer, T.; Rassow, J.; Kunau, W. H.; Voos, W.; Pfanner, N. (2000-08-01). "Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role". Molecular and Cellular Biology 20 (16): 5879–5887. doi:10.1128/mcb.20.16.5879-5887.2000. ISSN 0270-7306. PMID 10913171.
- ↑ Moro, Fernando; Okamoto, Koji; Donzeau, Mariel; Neupert, Walter; Brunner, Michael (2002-03-01). "Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44". The Journal of Biological Chemistry 277 (9): 6874–6880. doi:10.1074/jbc.M107935200. ISSN 0021-9258. PMID 11733493.
- "Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane". The EMBO Journal 16 (9): 2205–16. May 1997. doi:10.1093/emboj/16.9.2205. PMID 9171336.
- "The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system". Cell 81 (7): 1085–93. June 1995. doi:10.1016/S0092-8674(05)80013-3. PMID 7600576.
- "Mechanisms of protein translocation into mitochondria". Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes 1422 (3): 235–54. November 1999. doi:10.1016/s0304-4157(99)00007-6. PMID 10548718.
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