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Literature summary extracted from

  • Sun, Y.; Thompson, M.; Lin, G.; Butler, H.; Gao, Z.; Thornburgh, S.; Yau, K.; Smith, D.A.; Shukla, V.K.
    Inositol 1,3,4,5,6-pentakisphosphate 2-kinase from maize: molecular and biochemical characterization (2007), Plant Physiol., 144, 1278-1291.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.158 cloning and expression in Escherichia coli Zea mays
2.7.1.158 expression in Escherichia coli Zea mays

General Stability

EC Number General Stability Organism
2.7.1.158 accumulation of soluble ZmIPK1 protein is very low under various growing temperatures and induction conditions, and the majority of the fusion protein is detected in inclusion bodies. Therefore, an alternative strategy using chaperone protein coexpression to enhance ZmIPK1 protein solubility is exploited. Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.158 0.119
-
 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
 Zea mays
2.7.1.158 0.119
-
 myo-inositol 1,3,4,5,6-pentakisphosphate
-
 Zea mays
2.7.1.158 0.119
-
 1D-myo-inositol 1,3,4,5,6-pentakisphosphate 400 microM of substrate ATP is used Zea mays

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.158 inclusion body The majority of fusion protein is detected. Zea mays 16234
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.158 48850
-
 predicted Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.158 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP Zea mays intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways 1D-myo-inositol hexakisphosphate + ADP phytic acid, in higher plants, phytic acid can mediate abscisic acid-induced guard cell closure by inactivating plasma membrane inward K+ conductance. During this process, phytic acid appears to act as an endomembrane calcium-releasing signal. ir
2.7.1.158 1D-myo-inositol 1,4,6-trisphosphate + ATP Zea mays relative substrate specificity 93.9% 1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
 ?
2.7.1.158 additional information Zea mays capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%) ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.158 Zea mays
-
-
-
2.7.1.158 Zea mays A4GWX8
-
-
2.7.1.158 Zea mays A4GWX8 Alignments of the leaf- and seed-derived cDNA sequences with ZmIPK1A define nine predicted exons and eight predicted introns in theZmIPK1 genomic sequence
-
2.7.1.158 Zea mays A6YH13
-
-
2.7.1.158 Zea mays A6YH13 contains a 31 bp deletion and a 7 bp polymorphism when compared to ZmIPK1A
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.158 a glutathione affinity column is used to capture intact GST-ZmIPK1. The purified GST-ZmIPK1 fusion is cleaved with thrombin and further purified by a sequential affinity and ion-exchange chromatography. ZmIPK1 protein is eluted at 0.1 M NaCl on a high resolution Mono Q column with an estimated purity of 95%. Identity of the purified protein is confirmed via trypsin digestion followed by matrix-assisted laser deposition/ionization (MALDI) time-of-flight mass spectrometry analysis and comparison of the MALDI fingerprint to the amino acid sequences deduced from ZmIPK1. Zea mays
2.7.1.158 expression in Escherichia coli Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.1.158 cob immature ear Zea mays
-
2.7.1.158 corn silk
-
 Zea mays
-
2.7.1.158 embryo mature Zea mays
-
2.7.1.158 embryo maturing, ZmIPK1A Zea mays
-
2.7.1.158 endosperm midstage, ZmIPK1A Zea mays
-
2.7.1.158 endosperm midstage Zea mays
-
2.7.1.158 leaf
-
 Zea mays
-
2.7.1.158 leaf a variety of alternative splicing products of ZmIPK1A are discovered in maize leaves and seeds Zea mays
-
2.7.1.158 leaf A variety of alternative splicing products of ZmIPK1A are discovered in maize leaves and seeds. The products are derived from alternative acceptor sites, alternative donor sites, and retained introns in the transcripts. Up to 50% of the ZmIPK1A transcripts in maize seeds and leaves have an interrupted open reading frame. One type of splicing product of ZmIPK1B is detected in roots. Zea mays
-
2.7.1.158 additional information A variety of alternative splicing products of ZmIPK1A are discovered in maize leaves and seeds. Products are derived from alternative acceptor sites, alternative donor sites, and retained introns in the transcripts. Up to 50% of the ZmIPK1A transcripts in maize seeds and leaves have an interrupted open reading frame. Zea mays
-
2.7.1.158 root
-
 Zea mays
-
2.7.1.158 root transcripts of ZmIPK1B were exclusively detected in roots Zea mays
-
2.7.1.158 root transcripts detected in ZmIPK1B Zea mays
-
2.7.1.158 seed
-
 Zea mays
-
2.7.1.158 seed a variety of alternative splicing products of ZmIPK1A are discovered in maize leaves and seeds, ZmIPK1A Zea mays
-
2.7.1.158 seed at 12 d after pollination Zea mays
-
2.7.1.158 silk ZmIPK1A Zea mays
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.158 0.625
-
-
 Zea mays

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.158 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways Zea mays 1D-myo-inositol hexakisphosphate + ADP phytic acid, in higher plants, phytic acid can mediate abscisic acid-induced guard cell closure by inactivating plasma membrane inward K+ conductance. During this process, phytic acid appears to act as an endomembrane calcium-releasing signal. ir
2.7.1.158 1D-myo-inositol 1,4,6-trisphosphate + ATP relative substrate specificity 93.9% Zea mays 1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
 ?
2.7.1.158 ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
 Zea mays ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
 ?
2.7.1.158 ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
 Zea mays ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
 ?
2.7.1.158 ATP + myo-inositol 1,3,4,5,6-pentakisphosphate
-
 Zea mays ADP + myo-inositol hexakisphosphate
-
 ?
2.7.1.158 ATP + myo-inositol 1,4,6-trisphosphate
-
 Zea mays ADP + inositol 1,2,4,6-tetrakisphosphate
-
 ?
2.7.1.158 additional information capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%) Zea mays ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.158 inositol 1,3,4,5,6-pentakisphosphate 2-kinase
-
 Zea mays
2.7.1.158 Ipk1
-
 Zea mays
2.7.1.158 ZmIPK1
-
 Zea mays
2.7.1.158 ZmIPK1A
-
 Zea mays
2.7.1.158 ZmIPK1A nearly identical paralog Zea mays
2.7.1.158 ZmIPK1A nearly identical paralog to ZmIPK1, genomic ZmIPK1A sequence contains only one EcoRI site Zea mays
2.7.1.158 ZmIPK1B
-
 Zea mays
2.7.1.158 ZmIPK1B nearly identical paralog Zea mays

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.158 30
-
 assay at Zea mays

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.158 7.5
-
 assay at Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.158 ATP
-
 Zea mays

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.1.158 Zea mays predicted
-
 7.8