Cloned (Comment) | Organism |
---|---|
expression of wild-type Saccharomyces cerevisiae Vip1 kinase domain and of mutant Vip1 fused to human GSTIP6K1 as GST-tagged proteins in bacteria | Homo sapiens |
expression of wild-type Saccharomyces cerevisiae Vip1 kinase domain and of mutant Vip1 fused to human GSTIP6K1 as GST-tagged proteins in bacteria | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of full-length recombinant human GSTIP6K1, plus either GST fusion constructs comprising residues 1-387 of the human VIP1/PPIP5K1 kinase domain or residues 1-535 of the ScVip1 kinase domain | Saccharomyces cerevisiae |
additional information | construction of full-length recombinant human GSTIP6K1, plus either Saccharomyces cerevisiae GST fusion constructs comprising residues 1-387 of the human VIP1/PPIP5K1 kinase domain or residues 1-535 of the ScVip1 kinase domain | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens | |
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP | Homo sapiens | - |
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP | - |
? | |
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP | Saccharomyces cerevisiae | - |
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP | - |
? | |
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP | Homo sapiens | - |
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP | Saccharomyces cerevisiae | - |
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP | Homo sapiens | - |
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP | Saccharomyces cerevisiae | - |
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant GST-tagged wild-type Saccharomyces cerevisiae Vip1 kinase domain and mutant Vip1 fused to human GSTIP6K1 from bacteria | Homo sapiens |
recombinant GST-tagged wild-type Saccharomyces cerevisiae Vip1 kinase domain and mutant Vip1 fused to human GSTIP6K1 from bacteria | Saccharomyces cerevisiae |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
H-1299 cell | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP | - |
Homo sapiens | 1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP | - |
? | |
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP | - |
Saccharomyces cerevisiae | 1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP | - |
? | |
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP | - |
Homo sapiens | 3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP | - |
Saccharomyces cerevisiae | 3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP | - |
Homo sapiens | 3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP | - |
Saccharomyces cerevisiae | 3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP | - |
? | |
additional information | recombinant Vip1 kinase domain catalyzes 5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate formation from inositol hexakisphosphate. NMR substrate and product analysis, overview | Homo sapiens | ? | - |
? | |
additional information | recombinant Vip1 kinase domain catalyzes 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate formation from inositol hexakisphosphate. NMR substrate and product analysis, overview | Saccharomyces cerevisiae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
diphosphoinositol pentakisphosphate kinase | - |
Homo sapiens |
diphosphoinositol pentakisphosphate kinase | - |
Saccharomyces cerevisiae |
More | the enzyme belongs to the VIP/diphosphoinositol pentakisphosphate kinase, PPIP5K, family of inositol phosphate kinases | Homo sapiens |
More | the enzyme belongs to the VIP/diphosphoinositol pentakisphosphate kinase, PPIP5K, family of inositol phosphate kinases | Saccharomyces cerevisiae |
PPIP5K | - |
Homo sapiens |
PPIP5K | - |
Saccharomyces cerevisiae |
VIP | - |
Homo sapiens |
VIP | - |
Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.2 | - |
assay at | Homo sapiens |
6.2 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens | |
ATP | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
evolution | positional specificity of the mammalian and yeast VIP/diphosphoinositol pentakisphosphate kinase family of inositol phosphate kinases, overview. The mammalian and yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, phylogenetic variability within the crown taxa in the structures of inositol pyrophosphates, overview | Homo sapiens |
evolution | positional specificity of the mammalian and yeast VIP/diphosphoinositol pentakisphosphate kinase family of inositol phosphate kinases, overview. The mammalian and yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, phylogenetic variability within the crown taxa in the structures of inositol pyrophosphates, overview | Saccharomyces cerevisiae |
physiological function | the yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, and convert inositol hexakisphosphate to 1/3-diphosphoinositol pentakisphosphate with determination of unequivocally 1/3,5-(PP)2-IP4 is the isomeric structure of the bis-diphosphoinositol tetrakisphosphate | Saccharomyces cerevisiae |