Protein-secreting ATPase
From Wikipedia the free encyclopedia
| protein-exporting ATPase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.3.50 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a protein-secreting ATPase (EC 3.6.3.50) is an enzyme that catalyzes the chemical reaction
- ATP + H2O 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 (protein-secreting).
See also[edit]
References[edit]
- Saier MH, Tam R, Reizer A, Reizer J (1994). "Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport". Mol. Microbiol. 11 (5): 841–7. doi:10.1111/j.1365-2958.1994.tb00362.x. PMID 8022262.
- Mecsas JJ, Strauss EJ (1996). "Molecular mechanisms of bacterial virulence: type III secretion and pathogenicity islands". Emerg. Infect. Dis. 2 (4): 270–88. doi:10.3201/eid0204.960403. PMC 2639918. PMID 8969244.
- Thomas JD, Reeves PJ, Salmond GP (1997). "The general secretion pathway of Erwinia carotovora subsp carotovora: analysis of the membrane topology of OutC and OutF". Microbiology. 143 (3): 713–20. doi:10.1099/00221287-143-3-713. PMID 9084158.
- Baker B, Zambryski P, Staskawicz B, Dinesh-Kumar SP (1997). "Signaling in plant-microbe interactions". Science. 276 (5313): 726–33. doi:10.1126/science.276.5313.726. PMID 9115193.
- Martinez A, Ostrovsky P, Nunn DN (1998). "Identification of an additional member of the secretin superfamily of proteins in Pseudomonas aeruginosa that is able to function in type II protein secretion". Mol. Microbiol. 28 (6): 1235–46. doi:10.1046/j.1365-2958.1998.00888.x. PMID 9680212.
- Schuch R, Maurelli AT (1999). "The Mxi-Spa Type III Secretory Pathway of Shigella flexneri Requires an Outer Membrane Lipoprotein, MxiM, for Invasin Translocation". Infect. Immun. 67 (4): 1982–91. PMC 96556. PMID 10085046.
