Enzymes
| UniProtKB help_outline | 2,392 proteins |
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- Name help_outline 6-diphospho-1D-myo-inositol pentakisphosphate Identifier CHEBI:230534 Charge -13 Formula C6H6O27P7 InChIKeyhelp_outline UPHPWXPNZIOZJL-XCMZKKERSA-A SMILEShelp_outline [C@H]1(OP([O-])(=O)[O-])[C@@H](OP([O-])(=O)[O-])[C@@H](OP([O-])(=O)[O-])[C@@H]([C@H]([C@@H]1OP(=O)([O-])[O-])OP(=O)([O-])[O-])OP(=O)(OP([O-])(=O)[O-])[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1D-myo-inositol hexakisphosphate Identifier CHEBI:58130 (Beilstein: 3886124) help_outline Charge -12 Formula C6H6O24P6 InChIKeyhelp_outline IMQLKJBTEOYOSI-GPIVLXJGSA-B SMILEShelp_outline [O-]P([O-])(=O)O[C@@H]1[C@H](OP([O-])([O-])=O)[C@H](OP([O-])([O-])=O)[C@@H](OP([O-])([O-])=O)[C@H](OP([O-])([O-])=O)[C@H]1OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,029 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:79703 | RHEA:79704 | RHEA:79705 | RHEA:79706 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| EC numbers help_outline |
Publications
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A structural expose of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop.
Wang H., Perera L., Jork N., Zong G., Riley A.M., Potter B.V.L., Jessen H.J., Shears S.B.
Structural snapshots of protein/ligand complexes are a prerequisite for gaining atomic level insight into enzymatic reaction mechanisms. An important group of enzymes has been deprived of this analytical privilege: members of the protein tyrosine phosphatase (PTP) superfamily with catalytic WPD-lo ... >> More
Structural snapshots of protein/ligand complexes are a prerequisite for gaining atomic level insight into enzymatic reaction mechanisms. An important group of enzymes has been deprived of this analytical privilege: members of the protein tyrosine phosphatase (PTP) superfamily with catalytic WPD-loops lacking the indispensable general-acid/base within a tryptophan-proline-aspartate/glutamate context. Here, we provide the ligand/enzyme crystal complexes for one such PTP outlier: Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1 (AtPFA-DSP1), herein unveiled as a regioselective and efficient phosphatase towards inositol pyrophosphate (PP-InsP) signaling molecules. Although the WPD loop is missing its canonical tripeptide motif, this structural element contributes to catalysis by assisting PP-InsP delivery into the catalytic pocket, for a choreographed exchange with phosphate reaction product. Subsequently, an intramolecular proton donation by PP-InsP substrate is posited to substitute functionally for the absent aspartate/glutamate general-acid. Overall, we expand mechanistic insight into adaptability of the conserved PTP structural elements. << Less
Nat. Commun. 13:2231-2231(2022) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Arabidopsis PFA-DSP-Type Phosphohydrolases Target Specific Inositol Pyrophosphate Messengers.
Gaugler P., Schneider R., Liu G., Qiu D., Weber J., Schmid J., Jork N., Haener M., Ritter K., Fernandez-Rebollo N., Giehl R.F.H., Trung M.N., Yadav R., Fiedler D., Gaugler V., Jessen H.J., Schaaf G., Laha D.
Inositol pyrophosphates are signaling molecules containing at least one phosphoanhydride bond that regulate a wide range of cellular processes in eukaryotes. With a cyclic array of phosphate esters and diphosphate groups around <i>myo</i>-inositol, these molecular messengers possess the highest ch ... >> More
Inositol pyrophosphates are signaling molecules containing at least one phosphoanhydride bond that regulate a wide range of cellular processes in eukaryotes. With a cyclic array of phosphate esters and diphosphate groups around <i>myo</i>-inositol, these molecular messengers possess the highest charge density found in nature. Recent work deciphering inositol pyrophosphate biosynthesis in <i>Arabidopsis</i> revealed important functions of these messengers in nutrient sensing, hormone signaling, and plant immunity. However, despite the rapid hydrolysis of these molecules in plant extracts, very little is known about the molecular identity of the phosphohydrolases that convert these messengers back to their inositol polyphosphate precursors. Here, we investigate whether <i>Arabidopsis</i> Plant and Fungi Atypical Dual Specificity Phosphatases (PFA-DSP1-5) catalyze inositol pyrophosphate phosphohydrolase activity. We find that recombinant proteins of all five <i>Arabidopsis</i> PFA-DSP homologues display phosphohydrolase activity with a high specificity for the 5-β-phosphate of inositol pyrophosphates and only minor activity against the β-phosphates of 4-InsP<sub>7</sub> and 6-InsP<sub>7</sub>. We further show that heterologous expression of <i>Arabidopsis</i> PFA-DSP1-5 rescues wortmannin sensitivity and deranged inositol pyrophosphate homeostasis caused by the deficiency of the PFA-DSP-type inositol pyrophosphate phosphohydrolase Siw14 in yeast. Heterologous expression in <i>Nicotiana benthamiana</i> leaves provided evidence that <i>Arabidopsis</i> PFA-DSP1 also displays 5-β-phosphate-specific inositol pyrophosphate phosphohydrolase activity <i>in planta</i>. Our findings lay the biochemical basis and provide the genetic tools to uncover the roles of inositol pyrophosphates in plant physiology and plant development. << Less
Biochemistry 61:1213-1227(2022) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.