Inositol Monophosphatase
From Proteopedia
(Difference between revisions)
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===FBPase=== | ===FBPase=== | ||
Under normal conditions the MJ0109 gene product preferentially metabolizes the second last major step in [http://en.wikipedia.org/wiki/Gluconeogenesis| gluconeogenesis], fructose-1,6-bisphosphate substrate to fructose-6-phosphate. Relative to its IMPase activity, the FBPase activity of MJ0109 is 1.63 times as active<ref name="rasmol"/>. This particular function was not immediately identified by genomic sequence alignment and was later determined using structual and kinetic analysis<ref name="rasmol"/>. FBPase K<sub>m</sub> and K<sub>cat</sub> at 85°C; 38±9μM and 7.0±0.4/s, respectively<ref name="rasmol"/>. | Under normal conditions the MJ0109 gene product preferentially metabolizes the second last major step in [http://en.wikipedia.org/wiki/Gluconeogenesis| gluconeogenesis], fructose-1,6-bisphosphate substrate to fructose-6-phosphate. Relative to its IMPase activity, the FBPase activity of MJ0109 is 1.63 times as active<ref name="rasmol"/>. This particular function was not immediately identified by genomic sequence alignment and was later determined using structual and kinetic analysis<ref name="rasmol"/>. FBPase K<sub>m</sub> and K<sub>cat</sub> at 85°C; 38±9μM and 7.0±0.4/s, respectively<ref name="rasmol"/>. | ||
| + | ===FBPase/IMPase=== | ||
| + | An unusual phosphatase found in several hyperthermophilic organisms which has dual activity toward inositol monophosphate and fructose 1,6-bisphosphate<ref>PMID:11940584</ref>. | ||
===Inhibitors=== | ===Inhibitors=== | ||
As the dual activity indicates, the substrate specificity of this enzyme is particularly low. Proposed evolutionary cousins of this enzyme are regulated by [http://en.wikipedia.org/wiki/Adenosine_monophosphate| Adenosine monophosphate] and [http://en.wikipedia.org/wiki/Fructose_2,6-bisphosphate| Fructose 2,6-bisphosphate]. However, there are no such allosteric regulatory binding sites on the MJ0109 protein. Additionally, ''M. jannaschii'' IMPase has a [http://en.wikipedia.org/wiki/IC50| IC50] for Li+ of >150mM, compared to the Li+ IC50 of human IMPase <1mM<ref name="rasmol"/>. | As the dual activity indicates, the substrate specificity of this enzyme is particularly low. Proposed evolutionary cousins of this enzyme are regulated by [http://en.wikipedia.org/wiki/Adenosine_monophosphate| Adenosine monophosphate] and [http://en.wikipedia.org/wiki/Fructose_2,6-bisphosphate| Fructose 2,6-bisphosphate]. However, there are no such allosteric regulatory binding sites on the MJ0109 protein. Additionally, ''M. jannaschii'' IMPase has a [http://en.wikipedia.org/wiki/IC50| IC50] for Li+ of >150mM, compared to the Li+ IC50 of human IMPase <1mM<ref name="rasmol"/>. | ||
=Evolution= | =Evolution= | ||
It is generally well received that [http://en.wikipedia.org/wiki/Hyperthermophile| hyperthermophiles] are near the oldest phyletic group, with a very slow rate of evolution<ref name="rasmol"/>. This is due to the rather unforgiving environment toward mutations of these microbes. Given that the MJ0109 protein lacks substrate specificity and regulatory sites, and possess activity of two separate pathways in Eukaryotes; it is a reasonable assumption that this enzyme is an evolutionary snap shot of an original phosphatase approximation<ref name="rasmol"/>. | It is generally well received that [http://en.wikipedia.org/wiki/Hyperthermophile| hyperthermophiles] are near the oldest phyletic group, with a very slow rate of evolution<ref name="rasmol"/>. This is due to the rather unforgiving environment toward mutations of these microbes. Given that the MJ0109 protein lacks substrate specificity and regulatory sites, and possess activity of two separate pathways in Eukaryotes; it is a reasonable assumption that this enzyme is an evolutionary snap shot of an original phosphatase approximation<ref name="rasmol"/>. | ||
| + | |||
| + | ==3D Structures of Inositol Monophosphatase== | ||
| + | [[Inositol monophosphatase 3D structures]] | ||
| + | |||
</StructureSection> | </StructureSection> | ||
=3D Structures of Inositol Monophosphatase= | =3D Structures of Inositol Monophosphatase= | ||
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*Inositol monophosphatase | *Inositol monophosphatase | ||
| - | **[[2bji]] – IMP 1 - bovine<br /> | ||
**[[2ddk]], [[2czk]], [[2fvz]] – hIMP 2 – human<br /> | **[[2ddk]], [[2czk]], [[2fvz]] – hIMP 2 – human<br /> | ||
**[[4as4]] – hIMP 1<br /> | **[[4as4]] – hIMP 1<br /> | ||
**[[1imf]] – hIMP<br /> | **[[1imf]] – hIMP<br /> | ||
| + | **[[2bji]] – IMP 1 - bovine<br /> | ||
**[[4as5]] – IMP 1 - mouse<br /> | **[[4as5]] – IMP 1 - mouse<br /> | ||
| - | **[[2qfl]] – IMP – ''Escherichia coli''<br /> | + | **[[2qfl]], [[6ib7]] – IMP – ''Escherichia coli''<br /> |
**[[2p3n]], [[2p3v]] – IMP – ''Thermotoga maritima''<br /> | **[[2p3n]], [[2p3v]] – IMP – ''Thermotoga maritima''<br /> | ||
**[[2pcr]] – IMP – ''Aquifex aeolicus''<br /> | **[[2pcr]] – IMP – ''Aquifex aeolicus''<br /> | ||
| Line 40: | Line 46: | ||
**[[4n81]] - IMP - ''Zymomonas mobilis''<br /> | **[[4n81]] - IMP - ''Zymomonas mobilis''<br /> | ||
**[[5eqa]] – MtIMP – ''Medicago truncatula''<br /> | **[[5eqa]] – MtIMP – ''Medicago truncatula''<br /> | ||
| + | **[[5zhh]] - IMP - ''Anabaena''<br /> | ||
*Inositol monophosphatase binary complex | *Inositol monophosphatase binary complex | ||
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**[[1ima]], [[1imb]] - hIMP + inositol-1-phosphate<br /> | **[[1ima]], [[1imb]] - hIMP + inositol-1-phosphate<br /> | ||
**[[1ime]] – hIMP + Ca<br /> | **[[1ime]] – hIMP + Ca<br /> | ||
| + | **[[6giu]] – hIMP + lithium mimetic<br /> | ||
| + | **[[6gj0]] – hIMP + Mn<br /> | ||
**[[1g0h]], [[1g0i]] - MjIMP + inositol-1-phosphate<br /> | **[[1g0h]], [[1g0i]] - MjIMP + inositol-1-phosphate<br /> | ||
**[[3ryd]] – SaIMP + Ca<br /> | **[[3ryd]] – SaIMP + Ca<br /> | ||
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**[[5eq7]], [[5t3j]] – MtIMP + phosphate <br /> | **[[5eq7]], [[5t3j]] – MtIMP + phosphate <br /> | ||
**[[5eq8]], [[5eq9]] – MtIMP + histidinol<br /> | **[[5eq8]], [[5eq9]] – MtIMP + histidinol<br /> | ||
| + | **[[6ib8]] – EcIMP + NUSA<br /> | ||
*Inositol monophosphatase ternary complex | *Inositol monophosphatase ternary complex | ||
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**[[5djk]] - MtIMP + Ca + phosphate<br /> | **[[5djk]] - MtIMP + Ca + phosphate<br /> | ||
**[[5djh]], [[5dji]] - MtIMP + AMP + Mg + phosphate<br /> | **[[5djh]], [[5dji]] - MtIMP + AMP + Mg + phosphate<br /> | ||
| + | |||
| + | *Fructose-1,6-bisphosphatase/inositol-1- monophosphatase | ||
| + | |||
| + | **[[1lbw]] – AfFBPase/IMPase – Archaeoglobus fulgidus<br /> | ||
| + | **[[6b65]] – AfFBPase/IMPase (mutant) <br /> | ||
| + | **[[6b61]], [[6b63]] – AfFBPase/IMPase + Asp <br /> | ||
| + | **[[6b64]] – AfFBPase/IMPase (mutant) + Asp <br /> | ||
| + | **[[6b5z]] – AfFBPase/IMPase + inositol + Asp <br /> | ||
| + | **[[6b60]], [[6b62]] – AfFBPase/IMPase + Glu <br /> | ||
| + | **[[6b66]] – AfFBPase/IMPase (mutant) + Glu <br /> | ||
| + | **[[1lbx]] – AfFBPase/IMPase + inositol-1-phosphate + Ca <br /> | ||
| + | **[[1lbz]] – AfFBPase/IMPase + fructose-1,6-bisphosphate + Ca <br /> | ||
| + | **[[1lby]] – AfFBPase/IMPase + fructose-6-phosphate + PO4 + Mn <br /> | ||
| + | |||
}} | }} | ||
=References= | =References= | ||
Revision as of 07:12, 29 August 2019
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3D Structures of Inositol Monophosphatase
Updated on 29-August-2019
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 1.9 Stec B, Yang H, Johnson KA, Chen L, Roberts MF. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561 doi:10.1038/80968
- ↑ 2.0 2.1 Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200
- ↑ Bult CJ, White O, Olsen GJ, Zhou L, Fleischmann RD, Sutton GG, Blake JA, FitzGerald LM, Clayton RA, Gocayne JD, Kerlavage AR, Dougherty BA, Tomb JF, Adams MD, Reich CI, Overbeek R, Kirkness EF, Weinstock KG, Merrick JM, Glodek A, Scott JL, Geoghagen NS, Venter JC. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science. 1996 Aug 23;273(5278):1058-73. PMID:8688087
- ↑ Chen L, Spiliotis ET, Roberts MF. Biosynthesis of Di-myo-inositol-1,1'-phosphate, a novel osmolyte in hyperthermophilic archaea. J Bacteriol. 1998 Aug;180(15):3785-92. PMID:9683472
- ↑ Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200
