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Literature summary extracted from

  • Gonzalez, B.; Schell, M.J.; Letcher, A.J.; Veprintsev, D.B.; Irvine, R.F.; Williams, R.L.
    Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase (2004), Mol. Cell, 15, 689-701.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.1.127 Calmodulin i.e. CaM, regulatory function, in concert with Ca2+ Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.127 expression of His6-tagged fragment comprising residues 151-461 in Escherichia coli, expression of wild-type and mutant cDNA fragments encoding for residues 187-461 of the catalytic domain of isozyme A as unlabeled or selenomethionine-labeled GST fusion proteins in Escherichia coli strains C41(DE3) and B834(DE3) Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.127 purified recombinant unlabeled or selennomethionine-labeled wild-type and mutant catalytic domain residues 187-461 free or complexed to ATP, substrate, and product, automated sitting drop vapour diffusion method, 17°C, 0.001 ml protein solution over reservoir solution containing 0.83-0.85 M tri-sodium citrate, 0.1 M Tris-HCl, pH 8.0, and 0.1 M NaCl, heavy atom derivative, substrates, or products complex formation by addition and removal of 0.001 ml of 2 M Li2SO4 and 100 mM Tris-HCl, pH 8.0, 4°C, containing the relevant compound, i.e. 3 mM ATP, 3 mM MnCl2, or 5 mM 1D-myo-inositol 1,3,4,5-tetrakisphosphate, for 7times, and final soaking for 2.5 h, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.127 A187S crystal structure determination and analysis Homo sapiens
2.7.1.127 D262A 14% of wild-type enzyme activity Homo sapiens
2.7.1.127 D262N 12% of wild-type enzyme activity Homo sapiens
2.7.1.127 D416A inactive mutant Homo sapiens
2.7.1.127 K199A 80% of wild-type enzyme activity Homo sapiens
2.7.1.127 R391A 0.5% of wild-type enzyme activity Homo sapiens
2.7.1.127 R391D inactive mutant Homo sapiens
2.7.1.127 W188A 44% of wild-type enzyme activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.127 1D-myo-inositol 1,4,5-trisphosphate substrate inhibition of the catalytic domain Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.127 Ca2+ regulatory function in concert with calmodulin Homo sapiens
2.7.1.127 Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.127 ATP + 1D-myo-inositol 1,4,5-trisphosphate Homo sapiens
-
 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.127 Homo sapiens
-
 isozyme A
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.127 His6-tagged fragment comprising residues 151-461 from Escherichia coli by nickel affinity chromatography, unlabeled or selenomethionine-labeled recombinant residues 185-459 of the catalytic domain of isozyme A fused to GST from Escherichia coli by glutathione affinity chromatography, removal of the GST-tag by recombinant TEV protease, further purification by a heparin affinity chromatography, and gel filtration Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.127 ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate catalytic mechanism, ATP, substrate and product binding Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.127 ATP + 1D-myo-inositol 1,4,5-trisphosphate
-
 Homo sapiens ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
 ?
2.7.1.127 ATP + 1D-myo-inositol 1,4,5-trisphosphate substrate and product binding site structure Homo sapiens ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.127 More the enzyme possesses a DCK264 motif, an IP-lobe G266-G329, and an IDFG motif Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.1.127 inositol 1,4,5-trisphosphate 3-kinase
-
 Homo sapiens
2.7.1.127 More the enzyme belongs tot he IPK family, structure comparisons Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.127 ATP binding site structure, role of ATP-binding in the catalytic mechanism and substrate inhibition of the catalytic domain Homo sapiens