グリセロホスホイノシトールイノシトールホスホジエステラーゼ
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- inositol 1,2-cyclic phosphate 2-phosphohydrolase
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/06/26 07:23:28」(JST)
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| glycerophosphoinositol inositolphosphodiesterase |
| Identifiers |
| EC number |
3.1.4.43 |
| CAS number |
9076-91-9 |
| 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 |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
In enzymology, a glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction
- 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O glycerol + 1D-myo-inositol 1-phosphate
Thus, the two substrates of this enzyme are 1-(sn-glycero-3-phospho)-1D-myo-inositol and H2O, whereas its two products are glycerol and 1D-myo-inositol 1-phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is 1-(sn-glycero-3-phospho)-1D-myo-inositol inositolphosphohydrolase. Other names in common use include 1,2-cyclic-inositol-phosphate phosphodiesterase, D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase, D-inositol 1,2-cyclic phosphate 2-phosphohydrolase, D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase, 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, and inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase.
This enzyme 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, was reported to be identical to annexin III [Ross et al., Science, 248: 605-607, 1990]. Sekar et al. [J Biol. Chem. 271: 8295-8299, 1996] clearly demonstrated the dissociation of 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase activity from annexin III. Perron et al. [J. Biol. Chem. 272:11321-11326, 1997] confirmed based on structural studies that annexin III did not possess an enzymatic activity. While physiological significance of this enzymatic activity is still not clear, Sekar et al. [Biochem. Mol. Med. 61:95-100, 1007] reported over 10-fold increased release of this enzymatic activity in several patients admitted to the hospital's intensive care unit.
References
- Dawson RM, Hemington N (1977). "A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol". Biochem. J. 162 (2): 241–5. PMC 1164595. PMID 192216.
- Dawson RM, Clarke N (1972). "D-myoinositol 1:2-cyclic phosphate 2-phosphohydrolase". Biochem. J. 127 (1): 113–8. PMC 1178565. PMID 4342209.
- Dawson RM, Clarke NG (1973). "A comparison of D-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney". Biochem. J. 134 (1): 59–67. PMC 1177787. PMID 4353088.
- Ross TS, Majerus PW (1991). "Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase. Substrate specificity and regulation of activity by phospholipids, metal ion chelators, and inositol 2-phosphate". J. Biol. Chem. 266 (2): 851–6. PMID 1845995.
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Hydrolase: esterases (EC 3.1)
|
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3.1.1: Carboxylic
ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
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| 3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
- 4-hydroxybenzoyl-CoA thioesterase
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| 3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Protein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Protein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
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| 3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
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| 3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
| 3.1.11-16: Exonuclease |
| Exodeoxyribonuclease |
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| Exoribonuclease |
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| 3.1.21-31: Endonuclease |
| Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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|
| Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
|
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| either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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Enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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English Journal
- New members of the mammalian glycerophosphodiester phosphodiesterase family: GDE4 and GDE7 produce lysophosphatidic acid by lysophospholipase D activity.
- Ohshima N1, Kudo T2, Yamashita Y2, Mariggiò S3, Araki M1, Honda A2, Nagano T2, Isaji C1, Kato N2, Corda D3, Izumi T1, Yanaka N4.
- The Journal of biological chemistry.J Biol Chem.2014 Dec 20. pii: jbc.M114.614537. [Epub ahead of print]
- The known mammalian glycerophosphodiester phosphodiesterases (GP-PDEs) hydrolyze glycerophosphodiesters. In this study, two novel members of the mammalian GP-PDE family, GDE4 and GDE7, were isolated and the molecular basis of mammalian GP-PDEs was further explored. The GDE4 and GDE7 sequences are hi
- PMID 25528375
- A novel pathway for the synthesis of inositol phospholipids uses CDP-inositol as donor of the polar head group.
- Jorge CD1, Borges N, Santos H.
- Environmental microbiology.Environ Microbiol.2014 Dec 4. doi: 10.1111/1462-2920.12734. [Epub ahead of print]
- We describe a novel biosynthetic pathway for glycerophosphoinositides in Rhodothermus marinus in which inositol is activated by CTP; this is unlike all known pathways, which involve activation of the lipid group instead. This work was motivated by the detection in the R. marinus genome of a gene wit
- PMID 25472423
- Reproducible surface-enhanced Raman quantification of biomarkers in multicomponent mixtures.
- De Luca AC1, Reader-Harris P, Mazilu M, Mariggiò S, Corda D, Di Falco A.
- ACS nano.ACS Nano.2014 Mar 25;8(3):2575-83. doi: 10.1021/nn406200y. Epub 2014 Feb 19.
- Direct and quantitative detection of unlabeled glycerophosphoinositol (GroPIns), an abundant cytosolic phosphoinositide derivative, would allow rapid evaluation of several malignant cell transformations. Here we report label-free analysis of GroPIns via surface-enhanced Raman spectroscopy (SERS) wit
- PMID 24524333
Related Links
- In enzymology, a glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43 ) is an enzyme that catalyzes the chemical reaction. 1-(sn-glycero-3-phospho)-1D -myo-inositol + H2O \rightleftharpoons glycerol + 1D-myo-inositol 1-phosphate ...
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