This article includes a list of references, related reading, or external links, but its sources remain unclear because it lacks inline citations. (May 2021) |
The enzyme mannitol-1-phosphatase (EC 3.1.3.22) catalyzes the reaction
mannitol-1-phosphatase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.3.22 | ||||||||
CAS no. | 9055-29-2 | ||||||||
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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- D-mannitol 1-phosphate + H2O D-mannitol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is D-mannitol-1-phosphate phosphohydrolase. This enzyme is also called mannitol-1-phosphate phosphatase. This enzyme participates in fructose and mannose metabolism.
References
edit- Rumpho ME, Edwards GE, Loescher WH (1983). "A Pathway for Photosynthetic Carbon Flow to Mannitol in Celery Leaves : Activity and Localization of Key Enzymes". Plant Physiol. 73 (4): 869–873. doi:10.1104/pp.73.4.869. PMC 1066569. PMID 16663332.
- Yamada H, Okamoto K, Kodama K, Noguchi F, Tanaka S (May 1961). "Enzymatic studies on mannitol formation by Piricularia oryzae". J. Biochem. 49. Tokyo: 404–410. doi:10.1093/oxfordjournals.jbchem.a127317. PMID 13787089.