“Inositol-phosphate phosphatase”的意思、由来-开放百科全书

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Inositol-phosphate phosphatase

释义

Nomenclature
References

{{enzyme
| Name = inositol-1(or 4)-monophosphatase
| EC_number = 3.1.3.25
| CAS_number = 37184-63-7
| IUBMB_EC_number = 3/1/3/25
| GO_code = 0008934
| image = 2czi.jpg
| width = 270
| caption = Inositol monophosphatase 2, dimer, Human
}}

In enzymology, an inositol-phosphate phosphatase ({{EC number|3.1.3.25}}) is an enzyme that catalyzes the chemical reaction

myo-inositol phosphate + H₂O myo-inositol + phosphate

Thus, the two substrates of this enzyme are myo-inositol phosphate and H₂O, whereas its two products are myo-inositol and phosphate.

This enzyme participates in 3 metabolic pathways: streptomycin biosynthesis, inositol phosphate metabolism, and phosphatidylinositol signaling system.

Nomenclature

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is myo-inositol-phosphate phosphohydrolase. Other names in common use include:

myo-inositol-1(or 4)-monophosphatase,
inositol 1-phosphatase,
L-myo-inositol-1-phosphate phosphatase,
myo-inositol 1-phosphatase,
inositol phosphatase,
inositol monophosphate phosphatase,
inositol-1(or 4)-monophosphatase,
myo-inositol-1(or 4)-phosphate phosphohydrolase,
myo-inositol monophosphatase, and
myo-inositol-1-phosphatase.

References

{{cite journal | author = Eisenberg F Jr | date = 1967 | title = D-myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis | journal = J. Biol. Chem. | volume = 242 | pages = 1375–82 | pmid = 4290245 | issue = 7 }}
{{cite journal | author = Shute JK | date = 1988 | title = The purification and properties of myo-inositol monophosphatase from bovine brain | journal = Biochem. J. | volume = 249 | pages = 883–9 | pmid = 2833231 | last2 = Ragan | first2 = CI | last3 = Watling | first3 = KJ | last4 = Aspley | first4 = S | last5 = Jackson | first5 = RG | last6 = Reid | first6 = GG | last7 = Gani | first7 = D | last8 = Shute | first8 = JK | issue = 3 | pmc = 1148789 }}
{{cite journal |vauthors=Hallcher LM, Sherman WR | date = 1980 | title = The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain | journal = J. Biol. Chem. | volume = 255 | pages = 10896–901 | pmid = 6253491 | issue = 22 }}
{{cite journal |vauthors=Yoshikawa T, Turner G, Esterling LE, Sanders AR, Detera-Wadleigh SD | date = 1997 | title = A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a susceptibility region for bipolar disorder | journal = Mol. Psychiatry | volume = 2 | pages = 393–7 | pmid = 9322233 | doi = 10.1038/sj.mp.4000325 | issue = 5 }}
Cockcroft, S. (Ed.), Biology of Phosphoinositides, Biology of Phosphoinositides, Oxford, 2000, p. 320-338.
{{cite journal |vauthors=Ackermann KE, Gish BG, Honchar MP, Sherman WR | date = 1987 | title = Evidence that inositol 1-phosphate in brain of lithium-treated rats results mainly from phosphatidylinositol metabolism | journal = Biochem. J. | volume = 242 | pages = 517–24 | pmid = 3036092 | issue = 2 | pmc = 1147736 }}

{{Phospholipid metabolism}}{{Esterases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{3.1-enzyme-stub}}

3 : EC 3.1.3|Enzymes of known structure|Biology of bipolar disorder

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