Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.4.24 extracted from

  • Lin, H.; Fridy, P.C.; Ribeiro, A.A.; Choi, J.H.; Barma, D.K.; Vogel, G.; Falck, J.R.; Shears, S.B.; York, J.D.; Mayr, G.W.
    Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases (2009), J. Biol. Chem., 284, 1863-1872.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.4.24

Cloned(Commentary)

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

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

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

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

Source Tissue Comment Organism Textmining
H-1299 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
 assay at Homo sapiens
6.2
-
 assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens
ATP
-
 Saccharomyces cerevisiae

General Information

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