EC |
2.4.1.250 |
Accepted name: |
D-inositol-3-phosphate glycosyltransferase |
Reaction: |
UDP-N-acetyl-α-D-glucosamine + 1D-myo-inositol 3-phosphate = 1-O-(2-acetamido-2-deoxy-α-D-glucopyranosyl)-1D-myo-inositol 3-phosphate + UDP |
Glossary: |
mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy-α-D-glucopyranosyl]-1D-myo-inositol |
Other name(s): |
mycothiol glycosyltransferases; MshA; UDP-N-acetyl-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase |
Systematic name: |
UDP-N-acetyl-α-D-glucosamine:1D-myo-inositol 3-phosphate α-D-glycosyltransferase (configuration-retaining) |
Comments: |
The enzyme, which belongs to the GT-B fold superfamily, catalyses the first dedicated reaction in the biosynthesis of mycothiol [1]. The substrate was initially believed to be inositol, but eventually shown to be D-myo-inositol 3-phosphate [2]. A substantial conformational change occurs upon UDP binding, which generates the binding site for D-myo-inositol 3-phosphate [3]. |
References: |
1. |
Newton, G.L., Koledin, T., Gorovitz, B., Rawat, M., Fahey, R.C. and Av-Gay, Y. The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA). J. Bacteriol. 185 (2003) 3476–3479. [PMID: 12754249] |
2. |
Newton, G.L., Ta, P., Bzymek, K.P. and Fahey, R.C. Biochemistry of the initial steps of mycothiol biosynthesis. J. Biol. Chem. 281 (2006) 33910–33920. [PMID: 16940050] |
3. |
Vetting, M.W., Frantom, P.A. and Blanchard, J.S. Structural and enzymatic analysis of MshA from Corynebacterium glutamicum: substrate-assisted catalysis. J. Biol. Chem. 283 (2008) 15834–15844. [PMID: 18390549] |
|
[EC 2.4.1.250 created 2010] |
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|
|
|
EC |
2.7.1.64 |
Accepted name: |
inositol 3-kinase |
Reaction: |
ATP + myo-inositol = ADP + 1D-myo-inositol 3-phosphate |
Other name(s): |
inositol-1-kinase (phosphorylating); myoinositol kinase; myo-inositol 1-kinase |
Systematic name: |
ATP:myo-inositol 1-phosphotransferase |
References: |
1. |
English, P.D., Dietz, M. and Albersheim, P. Myoinositol kinase: partial purification and identification of product. Science 151 (1966) 198–199. [PMID: 5907906] |
2. |
Loewus, M.W., Sasaki, K., Leavitt, A.C., Muscell, L., Sherman, W.R. and Loewus, F.A. Enantiomeric form of myo-inositol-1-phosphate produced by myo-inositol-1-phosphate synthase and myoinositol kinase in higher-plants. Plant Physiol. 70 (1982) 1661–1663. [PMID: 16662739] |
3. |
Stephens, L.R., Kay, R.R. and Irvine, R.F. A myo-inositol D-3 hydroxykinase activity in Dictyostelium. Biochem. J. 272 (1990) 201–210. [PMID: 2176081] |
|
[EC 2.7.1.64 created 1972, modified 2001] |
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|
|
|
EC |
2.7.1.68 |
Accepted name: |
1-phosphatidylinositol-4-phosphate 5-kinase |
Reaction: |
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate |
Glossary: |
1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P2
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P2 |
Other name(s): |
diphosphoinositide kinase; PIP kinase; phosphatidylinositol 4-phosphate kinase; phosphatidylinositol-4-phosphate 5-kinase; type I PIP kinase |
Systematic name: |
ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase |
Comments: |
This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P2 in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known. |
References: |
1. |
Kai, M., Salway, J.G. and Hawthorne, J.N. The diphosphoinositide kinase of rat brain. Biochem. J. 106 (1968) 791–801. [PMID: 4295336] |
2. |
Kai, M., Salway, J.G., Michell, R.H. and Hawthorne, J.N. The biosynthesis of triphosphoinositide by rat brain in vitro. Biochem. Biophys. Res. Commun. 22 (1966) 370–375. |
3. |
Rameh, L.E., Tolias, K.F., Duckworth, B.C. and Cantley, L.C. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390 (1997) 192–196. [PMID: 9367159] |
|
[EC 2.7.1.68 created 1972, modified 1980, modified 1982, modified 2002] |
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|
EC |
2.7.1.137 |
Accepted name: |
phosphatidylinositol 3-kinase |
Reaction: |
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate |
Glossary: |
1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P |
Other name(s): |
1-phosphatidylinositol 3-kinase; type III phosphoinositide 3-kinase; Vps34p; type I phosphatidylinositol kinase |
Systematic name: |
ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase |
Comments: |
One mammalian isoform is known. |
References: |
1. |
Whitman, M., Downes, C.P., Keeler, M., Keller, T. and Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332 (1988) 644–646. [PMID: 2833705] |
2. |
Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535–602. [PMID: 11395417] |
|
[EC 2.7.1.137 created 1992, modified 2002] |
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|
EC |
2.7.1.150 |
Accepted name: |
1-phosphatidylinositol-3-phosphate 5-kinase |
Reaction: |
ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate |
Glossary: |
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate = PtdIns(3,5)P2 |
Other name(s): |
type III PIP kinase; phosphatidylinositol 3-phosphate 5-kinase |
Systematic name: |
ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase |
References: |
1. |
Cooke, F.T., Dove, S.K., McEwen, R.K., Painter, G., Holmes, A.B., Hall, M.N., Michell, R.H. and Parker, P.J. The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae. Curr. Biol. 9 (1998) 1219–1222. [PMID: 9811604] |
|
[EC 2.7.1.150 created 2002] |
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|
EC |
2.7.1.153 |
Accepted name: |
phosphatidylinositol-4,5-bisphosphate 3-kinase |
Reaction: |
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate |
Glossary: |
1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P2
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P2
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate = PtdIns(3,4,5)P3 |
Other name(s): |
type I phosphoinositide 3-kinase |
Systematic name: |
ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase |
Comments: |
This enzyme also catalyses the phosphorylation of PtdIns4P to PtdIns(3,4)P2, and of PtdIns to PtdIns3P. Four mammalian isoforms are known to exist. |
References: |
1. |
Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535–602. [PMID: 11395417] |
|
[EC 2.7.1.153 created 2002] |
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|
|
|
EC |
2.7.1.154 |
Accepted name: |
phosphatidylinositol-4-phosphate 3-kinase |
Reaction: |
ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate |
Glossary: |
1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P2 |
Other name(s): |
type II phosphoinositide 3-kinase; C2-domain-containing phosphoinositide 3-kinase; phosphoinositide 3-kinase |
Systematic name: |
ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase |
Comments: |
This enzyme also phosphorylates PtdIns to PtdIns3P. Three mammalian isoforms have been found to date. |
References: |
1. |
Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535–602. [PMID: 11395417] |
|
[EC 2.7.1.154 created 2002] |
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EC |
2.7.7.74 |
Accepted name: |
1L-myo-inositol 1-phosphate cytidylyltransferase |
Reaction: |
CTP + 1L-myo-inositol 1-phosphate = diphosphate + CDP-1L-myo-inositol |
Glossary: |
1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate |
Other name(s): |
CTP:inositol-1-phosphate cytidylyltransferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); IPCT (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); L-myo-inositol-1-phosphate cytidylyltransferase |
Systematic name: |
CTP:1L-myo-inositol 1-phosphate cytidylyltransferase |
Comments: |
In many organisms this activity is catalysed by a bifunctional enzyme. The cytidylyltransferase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) is absolutely specific for CTP and 1L-myo-inositol 1-phosphate. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3′-phosphate, a widespread organic solute in microorganisms adapted to hot environments. |
References: |
1. |
Rodrigues, M.V., Borges, N., Henriques, M., Lamosa, P., Ventura, R., Fernandes, C., Empadinhas, N., Maycock, C., da Costa, M.S. and Santos, H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189 (2007) 5405–5412. [PMID: 17526717] |
|
[EC 2.7.7.74 created 2011] |
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|
EC |
2.7.8.34 |
Accepted name: |
CDP-L-myo-inositol myo-inositolphosphotransferase |
Reaction: |
CDP-1L-myo-inositol + 1L-myo-inositol 1-phosphate = CMP + bis(1L-myo-inositol) 3,1′-phosphate 1-phosphate |
Glossary: |
1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate |
Other name(s): |
CDP-inositol:inositol-1-phosphate transferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); DIPPS (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)) |
Systematic name: |
CDP-1L-myo-inositol:1L-myo-inositol 1-phosphate myo-inositolphosphotransferase |
Comments: |
In many organisms this activity is catalysed by a bifunctional enzyme. The di-myo-inositol-1,3′-phosphate-1′-phosphate synthase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-1L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate, a widespread organic solute in microorganisms adapted to hot environments. |
References: |
1. |
Rodrigues, M.V., Borges, N., Henriques, M., Lamosa, P., Ventura, R., Fernandes, C., Empadinhas, N., Maycock, C., da Costa, M.S. and Santos, H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189 (2007) 5405–5412. [PMID: 17526717] |
|
[EC 2.7.8.34 created 2011] |
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|
EC |
2.7.8.39 |
Accepted name: |
archaetidylinositol phosphate synthase |
Reaction: |
CDP-2,3-bis-(O-phytanyl)-sn-glycerol + 1L-myo-inositol 1-phosphate = CMP + 1-archaetidyl-1D-myo-inositol 3-phosphate |
Glossary: |
1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP-2,3-di-(O-phytanyl)-sn-glycerol = CDP-archaeol
1-archaetidyl-1D-myo-inositol 3-phosphate = archaetidyl-myo-inositol 1-phosphate
|
Other name(s): |
AIP synthase |
Systematic name: |
CDP-2,3-bis-(O-phytanyl)-sn-glycerol:1L-myo-inositol 1-phosphate 1-sn-archaetidyltransferase |
Comments: |
Requires Mg2+ or Mn2+ for activity. The enzyme is involved in biosynthesis of archaetidyl-myo-inositol, a compound essential for glycolipid biosynthesis in archaea. |
References: |
1. |
Morii, H., Kiyonari, S., Ishino, Y. and Koga, Y. A novel biosynthetic pathway of archaetidyl-myo-inositol via archaetidyl-myo-inositol phosphate from CDP-archaeol and D-glucose 6-phosphate in methanoarchaeon Methanothermobacter thermautotrophicus cells. J. Biol. Chem. 284 (2009) 30766–30774. [PMID: 19740749] |
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[EC 2.7.8.39 created 2013] |
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|
EC |
3.1.3.64 |
Accepted name: |
phosphatidylinositol-3-phosphatase |
Reaction: |
1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate |
Glossary: |
inositol 1-phosphate = Ins-1-P
inositol 1,3-bisphosphate = Ins(1,3)P2
1-phosphatidyl-1D-myo-inositol = PtdIns
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P |
Other name(s): |
inositol-1,3-bisphosphate 3-phosphatase; inositol 1,3-bisphosphate phosphatase; inositol-polyphosphate 3-phosphatase; D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase; phosphatidyl-3-phosphate 3-phosphohydrolase |
Systematic name: |
1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase |
Comments: |
This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3)P2 to Ins-1-P. |
References: |
1. |
Lips, D.L. and Majerus, P.W. The discovery of a 3-phosphomonoesterase that hydrolyzes phosphatidylinositol 3-phosphate in NIH 3T3 cells. J. Biol. Chem. 264 (1989) 19911–19915. [PMID: 2555336] |
2. |
Caldwell, K.K., Lips, D.L., Bansal, V.S. and Majerus, P.W. Isolation and characterization of two 3-phosphatases that hydrolyze both phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate. J. Biol. Chem. 266 (1991) 18378–18386. [PMID: 1655747] |
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[EC 3.1.3.64 created 1992, [EC 3.1.3.65 created 1992, incorporated 2002], modified 2002]] |
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|
EC |
3.1.3.66 |
Accepted name: |
phosphatidylinositol-3,4-bisphosphate 4-phosphatase |
Reaction: |
1-phosphatidyl-myo-inositol 3,4-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate |
Glossary: |
inositol 3-phosphate = Ins-3-P
inositol 1,3-bisphosphate = Ins(1,3)P2
inositol 3,4-bisphosphate = Ins(3,4)P2
inositol 1,3,4-trisphosphate = Ins(1,3,4)P3
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P |
Other name(s): |
inositol-3,4-bisphosphate 4-phosphatase; D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase; phosphoinositide 4-phosphatase; inositol polyphosphate 4-phosphatase; inositol polyphosphate 4-phosphatase type II |
Systematic name: |
1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase |
Comments: |
Mg2+-independent. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4)P3 to Ins(1,3)P2. It also converts Ins(3,4)P2 into Ins-3-P. |
References: |
1. |
Howell, S., Barnaby, R.J., Rowe, T., Ragan, C.I. and Gee, N.S. Evidence for at least four different inositol bisphosphatases in bovine brain. Eur. J. Biochem. 183 (1989) 169–172. [PMID: 2546770] |
2. |
Norris, F.A., Auethavekiat, V. and Majerus, P.W. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270 (1995) 16128–16133. [PMID: 7608176] |
3. |
Norris, F.A., Atkins, R.C. and Majerus, P.W. The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J. Biol. Chem. 272 (1997) 23859–23864. [PMID: 9295334] |
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[EC 3.1.3.66 created 1992, modified 2002] |
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|
EC |
3.1.3.78 |
Accepted name: |
phosphatidylinositol-4,5-bisphosphate 4-phosphatase |
Reaction: |
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate |
Glossary: |
1-phosphatidyl-1D-myo-inositol 3-phosphate = PtdIns3P
1-phosphatidyl-1D-myo-inositol 4-phosphate = PtdIns4P
1-phosphatidyl-1D-myo-inositol 5-phosphate = PtdIns5P
1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate = PtdIns(3,4)P2
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate = PtdIns(3,5)P2
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = PtdIns(4,5)P2
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate = PtdIns(3,4,5)P3 |
Other name(s): |
phosphatidylinositol-4,5-bisphosphate 4-phosphatase I; phosphatidylinositol-4,5-bisphosphate 4-phosphatase II; type I PtdIns-4,5-P2 4-Ptase; type II PtdIns-4,5-P2 4-Ptase; IpgD; PtdIns-4,5-P2 4-phosphatase type I; PtdIns-4,5-P2 4-phosphatase type II; type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase; type 1 4-phosphatase |
Systematic name: |
1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 4-phosphohydrolase |
Comments: |
Two pathways exist in mammalian cells to degrade 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate [PtdIns(4,5)P2] [2]. One is catalysed by this enzyme and the other by EC 3.1.3.36, phosphoinositide 5-phosphatase, where the product is PtdIns4P. The enzyme from human is specific for PtdIns(4,5)P2 as substrate, as it cannot use PtdIns(3,4,5)P3, PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns5P, PtdIns4P or PtdIns3P [2]. In humans, the enzyme is localized to late endosomal/lysosomal membranes [2]. It can control nuclear levels of PtdIns5P and thereby control p53-dependent apoptosis [3]. |
References: |
1. |
Niebuhr, K., Giuriato, S., Pedron, T., Philpott, D.J., Gaits, F., Sable, J., Sheetz, M.P., Parsot, C., Sansonetti, P.J. and Payrastre, B. Conversion of PtdIns(4,5)P2 into PtdIns(5)P by the S. flexneri effector IpgD reorganizes host cell morphology. EMBO J. 21 (2002) 5069–5078. [PMID: 12356723] |
2. |
Ungewickell, A., Hugge, C., Kisseleva, M., Chang, S.C., Zou, J., Feng, Y., Galyov, E.E., Wilson, M. and Majerus, P.W. The identification and characterization of two phosphatidylinositol-4,5-bisphosphate 4-phosphatases. Proc. Natl. Acad. Sci. USA 102 (2005) 18854–18859. [PMID: 16365287] |
3. |
Zou, J., Marjanovic, J., Kisseleva, M.V., Wilson, M. and Majerus, P.W. Type I phosphatidylinositol-4,5-bisphosphate 4-phosphatase regulates stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 104 (2007) 16834–16839. [PMID: 17940011] |
4. |
Mason, D., Mallo, G.V., Terebiznik, M.R., Payrastre, B., Finlay, B.B., Brumell, J.H., Rameh, L. and Grinstein, S. Alteration of epithelial structure and function associated with PtdIns(4,5)P2 degradation by a bacterial phosphatase. J. Gen. Physiol. 129 (2007) 267–283. [PMID: 17389247] |
|
[EC 3.1.3.78 created 2008] |
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|
|
EC |
5.5.1.4 |
Accepted name: |
inositol-3-phosphate synthase |
Reaction: |
D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate |
Other name(s): |
myo-inositol-1-phosphate synthase; D-glucose 6-phosphate cycloaldolase; inositol 1-phosphate synthatase; glucose 6-phosphate cyclase; inositol 1-phosphate synthetase; glucose-6-phosphate inositol monophosphate cycloaldolase; glucocycloaldolase; 1L-myo-inositol-1-phosphate lyase (isomerizing) |
Systematic name: |
1D-myo-inositol-3-phosphate lyase (isomerizing) |
Comments: |
Requires NAD+, which dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1. Finally, the enzyme-bound NADH reconverts C-5 into the -CHOH- form. |
References: |
1. |
Eisenberg, F., Jr. D-Myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis. J. Biol. Chem. 242 (1967) 1375–1382. [PMID: 4290245] |
2. |
Sherman, W.R., Stewart, M.A. and Zinbo, M. Mass spectrometric study on the mechanism of D-glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase. J. Biol. Chem. 244 (1969) 5703–5708. [PMID: 4310603] |
3. |
Barnett, J.E.G. and Corina, D.L. The mechanism of glucose 6-phosphate-D-myo-inositol 1-phosphate cyclase of rat testis. The involvement of hydrogen atoms. Biochem. J. 108 (1968) 125–129. [PMID: 4297937] |
4. |
Barnett, J.E.G., Rasheed, A. and Corina, D.L. Partial reactions of glucose 6-phosphate-1L-myo-inositol 1-phosphate cyclase. Biochem. J. 131 (1973) 21–30. [PMID: 4352864] |
|
[EC 5.5.1.4 created 1972, modified 2001] |
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