Manganese-transporting ATPase
manganese-transporting ATPase | |||||||||
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Identifiers | |||||||||
EC number | 3.6.3.35 | ||||||||
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 / EGO | ||||||||
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In enzymology, a manganese-transporting ATPase (EC 3.6.3.35) is an enzyme that catalyzes the chemical reaction
- ATP + H2O + Mn2+out ADP + phosphate + Mn2+in
The 3 substrates of this enzyme are ATP, H2O, and Mn2+, whereas its 3 products are ADP, phosphate, and Mn2+.
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 (manganese-importing). This enzyme is also called ABC-type manganese permease complex.
References
- Kuan G, Dassa E, Saurin W, Hofnung M, Saier MH (1995). "Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases". Res. Microbiol. 146 (4): 271–8. doi:10.1016/0923-2508(96)81050-3. PMID 7569321.
- Saier MH Jr (1998). "Advances in Microbial Physiology Volume 40; Chapter - Molecular Phylogeny as a Basis for the Classification of Transport Proteins from Bacteria, Archaea and Eukarya". Adv. Microb. Physiol. Advances in Microbial Physiology. 40: 81–136. doi:10.1016/S0065-2911(08)60130-7. ISBN 978-0-12-027740-7. PMID 9889977.
- Novak R, Braun JS, Charpentier E, Tuomanen E (1998). "Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa". Mol. Microbiol. 29 (5): 1285–96. doi:10.1046/j.1365-2958.1998.01016.x. PMID 9767595.
- Kolenbrander PE, Andersen RN, Baker RA, Jenkinson HF (1998). "The adhesion-associated sca operon in Streptococcus gordonii encodes an inducible high-affinity ABC transporter for Mn2+ uptake". J. Bacteriol. 180 (2): 290–5. PMC 106884. PMID 9440518.
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