Any feedback?
Information on EC 2.7.1.158 - inositol-pentakisphosphate 2-kinase
for references in articles please use BRENDA:EC2.7.1.158Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.158 inositol-pentakisphosphate 2-kinaseIUBMB Comments
The enzyme can also use Ins(1,4,5,6)P4 and Ins(1,4,5)P3 as substrate. Inositol hexakisphosphate (phytate) accumulates in storage protein bodies during seed development and, when hydrolysed, releases stored nutrients to the developing seedling before the plant is capable of absorbing nutrients from its environment .
Specify your search results
Word Map
- 2.7.1.158
- hexakisphosphate
- phytate
-
multikinase
- 1,2,3,4,5,6-hexakisphosphate
- tetrakisphosphate
-
5/6-kinase
- diagnostics
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
inositol kinase, atipk1, inositol 1,3,4,5,6-pentakisphosphate 2-kinase, inositol pentakisphosphate 2-kinase, gmipk1, ip5 2-k, scipk1, zmipk1a, zmipk1, stitpk1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CnIpk1
inositol 1,3,4,5,6-pentakisphosphate 2-kinase
inositol hexakisphosphate kinase 1
inositol pentakisphosphate 2-kinase
InsP6-kinase
IP5 2-K
IP5 2-kinase
IP6K
IP6K1
Ipk1
ZmIPK1A
ZmIPK1B
inositol pentakisphosphate 2-kinase
-
ZmIPK1A
nearly identical paralog to ZmIPK1, genomic ZmIPK1A sequence contains only one EcoRI site
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol 1,3,4,5,6-pentakisphosphate 2-phosphotransferase
The enzyme can also use Ins(1,4,5,6)P4 [2] and Ins(1,4,5)P3 [3] as substrate. Inositol hexakisphosphate (phytate) accumulates in storage protein bodies during seed development and, when hydrolysed, releases stored nutrients to the developing seedling before the plant is capable of absorbing nutrients from its environment [5].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
134093-01-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP
1D-myo-inositol hexakisphosphate + ADP
intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways
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
1D-myo-inositol 1,4,6-trisphosphate + ATP
1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
relative substrate specificity 93.9%
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,6-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
ATP + myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + myo-inositol hexakisphosphate
-
-
-
?
ATP + myo-inositol 1,4,6-trisphosphate
ADP + inositol 1,2,4,6-tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
Cryptococcus neoformans var. grubii ATCC 208821
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
Cryptococcus neoformans var. grubii CBS 10515
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
Cryptococcus neoformans var. grubii FGSC 9487
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the enzyme may be involved in both inositol hexakisphosphate formation in maturing seeds and ATP resynthesis in germinating seeds
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
it is suggested that the enzyme is necessary for yolk sac development or function. Loss of inositol 1,3,4,5,6-pentakisphosphate 2-kinase is lethal
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
rate-determining step in production of 1D-myo-inositol hexakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
cytoplasmic production of 1D-myo-inositol hexakisphosphate is sufficient for mediating the Gle1-mRNA export pathway
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the product 1D-myo-inositol hexakisphosphate plays a role in messenger RNA export
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
the predominant activity of StITPK1 is that of an InsP5-ADP phosphotransferase.
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
-
-
?
additional information
?
-
no activity with 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
-
?
additional information
?
-
phosphotransfer from 2-FAM-InsP5 (2-O-(2-(5-fluoresceinylcarboxy)aminoethyl)-myo-inositol 1,3,4,5,6-pentakisphosphate) to ADP by AtIP5 2-K
-
-
-
additional information
?
-
with inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) combined at a 1:20 ATP:ADP ratio, InsP6 is converted via Ins(1,3,4,5,6)P5 to Ins(3,4,5,6) P4 and/or Ins(1,4,5,6)P4 with concomitant generation of ATP
-
-
-
additional information
?
-
substrate binding structure, overview
-
-
-
additional information
?
-
Cryptococcus neoformans var. grubii ATCC 208821
substrate binding structure, overview
-
-
-
additional information
?
-
Cryptococcus neoformans var. grubii CBS 10515
substrate binding structure, overview
-
-
-
additional information
?
-
Cryptococcus neoformans var. grubii FGSC 9487
substrate binding structure, overview
-
-
-
additional information
?
-
binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
-
-
-
additional information
?
-
binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
-
-
-
additional information
?
-
-
binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
-
-
-
additional information
?
-
-
the enzyme changes its kinase activity towards 1D-myo-inositol hexakisphosphate at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate 1D-myo-inositol hexakisphosphate
-
-
?
additional information
?
-
mIP5 2-K active site and substrate recognition, overview. The adenine is strongly recognized through polar and hydrophobic interactions with both protein lobes and the hinge connecting them. In particular, it forms polar interactions with His14 and the backbones of Pro116 and Leu118. The ribose OHs interact with the C-lobe residues Glu136 and Arg209. The triphosphate moiety is tightly bound to the N-lobe of the enzyme through polar interactions and to the C-lobe through two magnesium ions. In particular, phosphate interaction with residue Arg-33, with a flexible loop (G-loop, residues Gly15-Ser20) and with an acidic residue (Asp437) through the magnesium ions, is conserved throughout the PK superfamily and is essential for nucleotide binding and kinase activity
-
-
-
additional information
?
-
-
mIP5 2-K active site and substrate recognition, overview. The adenine is strongly recognized through polar and hydrophobic interactions with both protein lobes and the hinge connecting them. In particular, it forms polar interactions with His14 and the backbones of Pro116 and Leu118. The ribose OHs interact with the C-lobe residues Glu136 and Arg209. The triphosphate moiety is tightly bound to the N-lobe of the enzyme through polar interactions and to the C-lobe through two magnesium ions. In particular, phosphate interaction with residue Arg-33, with a flexible loop (G-loop, residues Gly15-Ser20) and with an acidic residue (Asp437) through the magnesium ions, is conserved throughout the PK superfamily and is essential for nucleotide binding and kinase activity
-
-
-
additional information
?
-
-
the enzyme changes its kinase activity towards 1D-myo-inositol hexakisphosphate at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate 1D-myo-inositol hexakisphosphate
-
-
?
additional information
?
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
-
-
?
additional information
?
-
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
-
-
?
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%)
-
-
?
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%)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP
1D-myo-inositol hexakisphosphate + ADP
intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways
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
1D-myo-inositol 1,4,6-trisphosphate + ATP
1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
relative substrate specificity 93.9%
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
Cryptococcus neoformans var. grubii ATCC 208821
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
Cryptococcus neoformans var. grubii CBS 10515
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
Cryptococcus neoformans var. grubii FGSC 9487
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the enzyme may be involved in both inositol hexakisphosphate formation in maturing seeds and ATP resynthesis in germinating seeds
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
it is suggested that the enzyme is necessary for yolk sac development or function. Loss of inositol 1,3,4,5,6-pentakisphosphate 2-kinase is lethal
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
rate-determining step in production of 1D-myo-inositol hexakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
cytoplasmic production of 1D-myo-inositol hexakisphosphate is sufficient for mediating the Gle1-mRNA export pathway
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
-
the product 1D-myo-inositol hexakisphosphate plays a role in messenger RNA export
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
the predominant activity of StITPK1 is that of an InsP5-ADP phosphotransferase.
-
-
?
additional information
?
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
-
-
?
additional information
?
-
-
StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
-
-
?
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%)
-
-
?
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%)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Zn2+
mammalian IP5 2-Ks share a zinc-binding site with a distinct structure. Murine mIP5 2-K presents two zinc ions in its structure, one in the CIP-lobe (Zn1) and the other close to the hinge region (Zn2), binding structure, overview. The Zn1 site is formed by residues from two CIP lobe elements: Cys159, Cys162, and Cys181 from CIP-I and Cys291 from CIP-II. This site presents the typical zinc geometry and coordination. Zn1 is necessary for protein folding and stability
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1D-myo-inositol 1,4,6-trisphosphate
-
IC50: about 0.0007 mM. Potently reduces conversion of 1D-myo-inositol 1,4,5-trisphosphate to 1D-myo-inositol 1,4,5,6-tetrakisphosphate + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
purpurogallin
determination of ternary structure of AtIP5 2-K with purpurogallin and ADP, overview
additional information
high throughput screening of Arabidopsis thaliana inositol pentakisphosphate 2-kinase using an active site fluorescent probe, 2-FAM-InsP5 (2-O-(2-(5-fluoresceinylcarboxy)aminoethyl)-myo-inositol 1,3,4,5,6-pentakisphosphate (triethylammonium salt)), molecular docking calculations, overview
-
N2-(m-trifluoromethylbenzyl),N6-(p-nitrobenzyl)purine
-
selective inhibitor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Autoimmune Diseases
Inhibition of the Inositol Kinase Itpkb Augments Calcium Signaling in Lymphocytes and Reveals a Novel Strategy to Treat Autoimmune Disease.
Dehydration
Importance of inositols and their derivatives in cowpea under root dehydration: An omics perspective.
Diabetes Mellitus, Type 1
Urinary peptidome may predict renal function decline in type 1 diabetes and microalbuminuria.
Diabetes Mellitus, Type 1
Urine Inositol Pentakisphosphate 2-kinase and Changes in Kidney Structure in Early Diabetic Kidney Disease in Type 1 Diabetes.
Diabetic Nephropathies
Urine Inositol Pentakisphosphate 2-kinase and Changes in Kidney Structure in Early Diabetic Kidney Disease in Type 1 Diabetes.
Graft vs Host Disease
Inhibition of inositol kinase B controls acute and chronic graft-versus-host disease.
Herpes Zoster
Urinary peptidome may predict renal function decline in type 1 diabetes and microalbuminuria.
Infections
A role for inositol hexakisphosphate in the maintenance of basal resistance to plant pathogens.
Melanoma
Melanocyte-stimulating hormone (alpha-MSH) inhibits the growth of human malignant melanoma cells with the induction of phosphatidyl inositol and myo-inositol phosphate levels.
Neoplasms
The Protective and Immunomodulatory Effects of Fucoidan Against 7,12-Dimethyl benz[a]anthracene-Induced Experimental Mammary Carcinogenesis Through the PD1/PDL1 Signaling Pathway in Rats.
Neoplasms
Urinary peptidome may predict renal function decline in type 1 diabetes and microalbuminuria.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06681
1D-myo-inositol 1,3,4,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.05599
1D-myo-inositol 1,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.00055
1D-myo-inositol 1,4,5-triphosphate
-
about, cosubstrate: ATP
0.03372
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N238A, at pH 7.5 and 25°C
0.03979
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme K200A, at pH 7.5 and 25°C
0.04348
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme H196A, at pH 7.5 and 25°C
0.04453
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
0.0548
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R45A, at pH 7.5 and 25°C
0.05935
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R192A, at pH 7.5 and 25°C
0.06227
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R415A, at pH 7.5 and 25°C
0.06305
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.06305
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.07686
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme Y419A, at pH 7.5 and 25°C
0.0833
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N239A, at pH 7.5 and 25°C
0.119
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
400 microM of substrate ATP is used
0.04754
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.04754
1D-myo-inositol 3,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.07917
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4581
1D-myo-inositol 1,3,4,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.11
1D-myo-inositol 1,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.246
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N238A, at pH 7.5 and 25°C
0.265
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme N239A, at pH 7.5 and 25°C
0.279
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme K200A, at pH 7.5 and 25°C
0.367
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R192A, at pH 7.5 and 25°C
0.453
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R45A, at pH 7.5 and 25°C
0.569
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme H196A, at pH 7.5 and 25°C
0.645
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme R415A, at pH 7.5 and 25°C
0.694
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
mutant enzyme Y419A, at pH 7.5 and 25°C
0.734
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.734
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.736
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
0.105
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
0.105
1D-myo-inositol 3,4,5,6-tetrakisphosphate
wild type enzyme, at pH 7.5 and 25°C
0.549
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.7
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
16.5
1D-myo-inositol 1,3,4,5,6-pentakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
2.2
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
wild type enzyme, at pH 7.5 and 25°C
6.8
1D-myo-inositol 3,4,5,6-tetrakisphosphate
-
mutant enzyme E82C/S142C, at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
1D-myo-inositol 1,4,6-trisphosphate
Schizosaccharomyces pombe
-
IC50: about 0.0007 mM. Potently reduces conversion of 1D-myo-inositol 1,4,5-trisphosphate to 1D-myo-inositol 1,4,5,6-tetrakisphosphate + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
-
30°C: about 60% of maximal activity, 50°C: about 10% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Cryptococcus neoformans var. grubii ATCC 208821
Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Cryptococcus neoformans var. grubii CBS 10515
Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
Cryptococcus neoformans var. grubii FGSC 9487
Filobasidiella neoformans var. grubii, serotype A
UniProt
brenda
cv. Pusa 9712, collected from the Division of Genetics, IARI, New Delhi
UniProt
brenda
Alignments of the leaf- and seed-derived cDNA sequences with ZmIPK1A define nine predicted exons and eight predicted introns in theZmIPK1 genomic sequence
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of Solanum tuberosum protein in Escherichia coli
brenda
-
XA232, with a gene trap construct embedded in the inositol 1,3,4,5,6-pentakisphosphate 2-kinase gene
brenda
additional information
-
strong expression of AtIPK1 in male and female organs of flower buds
brenda
a variety of alternative splicing products of ZmIPK1A are discovered in maize leaves and seeds
brenda
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.
brenda
-
ventricular layer of neural tube, expressed at day 9.5 postcoitum
brenda
-
the ventricular layer of the neural tube, at day 9.5 postcoitum, 2-kinase is expressed in the notochord
brenda
-
at day 9.5 postcoitum, 2-kinase is expressed in the notochord
brenda
a variety of alternative splicing products of ZmIPK1A are discovered in maize leaves and seeds, ZmIPK1A
brenda
-
myotome of somites. At day 9.5 postcoitum, 2-kinase is expressed in the notochord
brenda
additional information
expression profile of GmIPK1 across different tissues and seed development stages
brenda
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.
brenda
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.
brenda
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.
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
preferentially localized in euchromatin and nucleoli, and colocalized with mRNA
brenda
The majority of fusion protein is detected.
brenda
-
spatial microheterogeneity in the intracellular localization of IP5K in NRK cells, COS7 cell and H1299 overexpressing EGFP-IP5K fusion proteins, also confirmed for the endogenous enzyme
brenda
additional information
-
the overexpressed IP5K shows locally high concentrations in discrete foci. IP5K is highly concentrated in stress granules
brenda
-
preferentially localized in euchromatin and nucleoli, and colocalized with mRNA
brenda
additional information
IPP2K is present in cell nuclei, where it colocalizes with mRNA in the nucleoli, whereas in the cytoplasm it is found principally in stress granules. Distribution of baseline urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase/creatinine (IPP2K/Cr) in women and men, overview
-
brenda
additional information
-
IPP2K is present in cell nuclei, where it colocalizes with mRNA in the nucleoli, whereas in the cytoplasm it is found principally in stress granules. Distribution of baseline urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase/creatinine (IPP2K/Cr) in women and men, overview
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
differential spatial and temporal expression profiling of gene GmIpk1 and its two homologues Glyma06g03310 and Glyma04g03310 in Glycine max
evolution
most residues involved in substrate binding and catalysis are conserved between mammal and plant IP5 2-Ks, but some differences in the inositide P1 and P3 coordination are observed. InmIP5 2-K, additional interactions with P1 are produced through the side chain of Lys173, a residue non-conserved with the plant IP5 2-Ks but absolutely conserved in mammal enzymes, whereas conservative substitutions can be observed in other vertebrates
evolution
the amino acid sequence of GmIPK1 shows much similarity with that of Phaseolus vulgaris and Cicer arietinum. It also shows the presence of the characteristic Ins_P5_2-kinase domain required for catalytic activity
malfunction
-
a functional Asp1 kinase domain abolishes invasive growth which is monopolar
malfunction
a loss-of-function mutant exhibits disturbed phosphate homeostasis and overaccumulated phosphate as a consequence of increased phosphate uptake activity and root-to-shoot phosphate translocation. The mutant also shows a phosphate deficiency-like root system architecture with reduced primary root and enhanced lateral root growth
malfunction
a mutant of inositol pentakisphosphate 2-kinase displays hypersensitivity to arsenate stress and less arsenate uptake when compared to the wild type enzyme
malfunction
cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance
malfunction
disruption of inositol pentakisphosphate 2-kinase profoundly influences cellular processes
malfunction
in contrast to wild-type IPK1, which is able to restore the phosphate content of the ipk1-1 mutant to wild-type level, both kinase-inactive IPK1 forms fail to complement excessive phosphate accumulation and PSR gene activation in ipk1-1. Although both ipk1-1 and itpk1 mutants exhibit decreased levels of InsP6 (phytate) and diphosphoinositol pentakisphosphate (PP-InsP5; InsP7), disruption of another ITPK family enzyme, ITPK4, which correspondingly causes depletion of InsP6 and InsP7, does not display similar phosphate-related phenotypes, which precludes these InsP species from being effectors. Notably, the level of D/L-Ins(3,4,5,6)P4 is concurrently elevated in both ipk1-1 and itpk1 mutants, which demonstrates a specific correlation with the misregulated phosphate phenotypes. The level of D/L-Ins(3,4,5,6)P4 is not responsive to phosphate starvation that instead manifests a shoot-specific increase in the InsP7 level. Misregulation of phosphate homeostasis in ipk1-1 is not caused by defective InsP6-mediated mRNA export. Neither of the kinase-inactive IPK1 mutants K168A and D368A complement the PSR-like RSA phenotypes (i.e. reduced primary root and enhanced lateral root growth) of ipk1-1 mutant. In addition to the decreased InsP6 level, levels of InsP7 and InsP8 are also reduced in ipk1-1 mutants
malfunction
urine inositol pentakisphosphate 2-kinase and changes in kidney structure in early diabetic kidney disease in type 1 diabetes. A higher prevalence of detectable urinary inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) in type 1 diabetes correlates with early renal function decline. Proximal tubule cells from people with type 1 diabetes and diabetic kidney disease (DKD) express more IPP2K compared with controls. Demographics and clinical characteristics by tertile of baseline urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase/creatinine (IPP2K/Cr), overview
malfunction
-
cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance
-
metabolism
genetic dissection of the roles for InsP and PP-InsP biosynthesis enzymes in regulation of phosphate homeostasis, overview
metabolism
inositol 1,3,4,5,6-pentakisphosphate 2-kinase catalyzes the terminal step in the phytic acid biosynthetic pathway
metabolism
inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) comprise a reversible metabolic cassette converting Ins(3,4,5,6)P4 into 5-InsP7 and back in a nucleotide-dependent manner. Ability of Arabidopsis inositol tris/tetrakisphosphate kinase 1 to discriminate between symmetric and enantiomeric substrates in the production of diverse symmetric and asymmetric myo-inositol phosphate and diphospho-myo-inositol phosphate (inositol diphosphate) products
metabolism
nositol 1,3,4,5,6-pentakisphosphate 2-kinase catalyzes the terminal step in the phytic acid biosynthetic pathway
physiological function
knock-out mutant cells are defective in nuclear mRNA export, cell morphology, polarized growth, and cell separation
physiological function
-
Asp1 kinase activity regulates cell-cell adhesion and increases resistance towards thiabendazole. The Asp1 kinase activity encoded by the N-terminal part of the protein is regulated negatively by the C-terminal domain of Asp1. Asp1 is a key regulator of the morphological switch via the cAMP protein kinase A
physiological function
the enzyme activity is required for cytoplasmic dynein transport
physiological function
the enzyme has important roles in growth and phosphate homeostasis
physiological function
association of urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) with the presence and progression of diabetic kidney disease (DKD) lesions. Inositol 6-phosphate is a key intracellular signaling molecule with roles in mRNA editing and chromatin remodeling
physiological function
GmIPK1 plays a significant role in phytate synthesis
physiological function
inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IP5 2-K) phosphorylates inositol pentakisphosphate (IP5) to produce inositol 1,2,3,4,5,6-hexakisphosphate (IP6), from ATP
physiological function
inositol pentakisphosphate 2-kinase catalyzes the phosphorylation of the axial 2-OH of myo-inositol 1,3,4,5,6-pentakisphosphate for de novo synthesis of myo-inositol hexakisphosphate
physiological function
the kinase activity of inositol pentakisphosphate 2-kinase (IPK1) is required for phytate (inositol hexakisphosphate, InsP6) synthesis, and is indispensable for maintaining phosphate homeostasis under phosphate-replete conditions. Inositol 1,3,4-trisphosphate 5/6-kinase 1 (ITPK1) plays an equivalent role. In addition to regulating the phosphate content, the kinase activity of IPK1 is also required for root system architecture
physiological function
-
the enzyme activity is required for cytoplasmic dynein transport
-
additional information
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
additional information
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
-
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
Cryptococcus neoformans var. grubii FGSC 9487
-
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
-
additional information
Cryptococcus neoformans var. grubii ATCC 208821
-
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
-
additional information
Cryptococcus neoformans var. grubii CBS 10515
-
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
-
Show AA Sequence and Transmembrane Helices (3687 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
monomer
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
monomer
Cryptococcus neoformans var. grubii ATCC 208821
-
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
-
monomer
Cryptococcus neoformans var. grubii CBS 10515
-
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
-
monomer
Cryptococcus neoformans var. grubii FGSC 9487
-
1 * 41000, there are four monomers in the asymmetric unit, but size-exclusion chromatographic analysis indicates that an estimated molecular weight of CnIpk1 corresponds to 41 kDa, which is equivalent to a monomer. The four monomers in the asymmetric unit do not form any noticeable oligomeric conformation in a symmetric manner, which indicated that CnIpk1 is a monomeric enzyme
-
additional information
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
additional information
Cryptococcus neoformans var. grubii ATCC 208821
-
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
-
additional information
Cryptococcus neoformans var. grubii CBS 10515
-
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
-
additional information
Cryptococcus neoformans var. grubii FGSC 9487
-
enzyme CnIpk1 exhibits two structural lobes: the N-terminal lobe (N-lobe, residues Met1-Glu134) and the C-terminal lobe (C-lobe, residues Ile146-Arg415) with an 11-residue loop between the lobes. Specifically, the N-lobe forms an alpha/beta fold with five antiparallel beta-strands in an 1-2-3-5-4 order and surrounding alpha-helices, structure overview
-
additional information
enzyme domain analysis from sequence, sequence comparisons
additional information
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
-
secondary structure prediction revealing that 74.46% of amino acids are in alpha-helix, whereas 57.64% of residues in beta-sheets and 12.19% in coil conformations, structure modeling, overview
additional information
peptide mapping, quantitative LC-selective reaction monitoring-MS (LC-SRM-MS) analysis
additional information
-
peptide mapping, quantitative LC-selective reaction monitoring-MS (LC-SRM-MS) analysis
additional information
mouse IP5 2-K folds in two lobes, N- and C-terminal lobes, connected by a hinge, thereby conserving the general fold scheme of PKs and IPKs, and in a similar way, both lobes coordinate the nucleotide between them. The N-lobe core forms a beta-sheet from five antiparallel beta-strands (beta1-beta5) showing two helical segments. The first helical segment (N-I) harbors alpha1, equivalent to the helix alphaC characterized in all protein kinases, whereas the second one (N-II) is a specific insertion different in every IPK subfamily. Structure comparisons
additional information
-
mouse IP5 2-K folds in two lobes, N- and C-terminal lobes, connected by a hinge, thereby conserving the general fold scheme of PKs and IPKs, and in a similar way, both lobes coordinate the nucleotide between them. The N-lobe core forms a beta-sheet from five antiparallel beta-strands (beta1-beta5) showing two helical segments. The first helical segment (N-I) harbors alpha1, equivalent to the helix alphaC characterized in all protein kinases, whereas the second one (N-II) is a specific insertion different in every IPK subfamily. Structure comparisons
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complexes with ADP and myo-Ins(1,3,4,5,6)P5, myo-InsP6, neo-InsP6, D-chiro-InsP6, or purpurogallin, sitting drop method, mixing of 5.0-7.5 mg/ml protein solution containing 2 mM ADP and 2 mM ligand with reservoir solution, containing 18 % w/v PEG 3350, 0.1 M bis-Tris propane, pH 6.5, and 2 mM MgCl2, in a 1:1 ratio, and equilibration against 0.05 ml of reservoir solution, 16°C, microseeding X-ray diffraction structure determination and analysis, molecular replacement and modeling
purified recombinant detagged wild-type and mutant enzymes in complex with IP6 and ADP, sitting drop vapor diffusion method, mixing of 20 mg/ml protein solution with crystallization solution containing 0.1 M MES, pH 6.0, 2.1-2.3 M ammonium sulfate, and 10-50 mM TCEP, 22°C, 20% v/v ethylene glycol is used as a cryoprotectant, X-ray diffraction structure determination and analysis at 2.35-2.5 A resolution
purified recombinant detagged enzyme, sitting drop vapour diffusion, mixing of 250 nl of 5-6 mg/ml protein solution with 250 nl of crystallization solution containing 0.2 M MgCl2, 0.1 M MES, pH 6.25, and 18% v/v PEG 6000 for insect cell-expressed enzyme, and 0.2 M MgCl2, 0.1 M MES, pH 6.25, and 12% v/v PEG 6000 for bacteria-expressed enzyme, equilibration against 0.065 ml of crystallization solution as reservoir, method screening and optimization, X-ray diffraction structure determination and analysis at resolution of 4.3 A (Escherichia coli expression) and 4.0 A (insect cell expression), modeling
purified recombinant truncated enzyme lacking the 21 C-terminal residues (DELTAC-mIP5 2-K) in complex with IP5 and ATP or with IP6, X-ray diffraction structure determination and analysis at 2.4-3.2 A resolution. mIP5 2-K cyrstals are not obtained in the absence of inositide, structure for mIP5 2-K in the presence of one or both ligands, forming binary complexes (IP6) or ternary complexes
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D368A
E82C/S142C
-
the mutant exhibits a dithiothreitol-sensitive 5fold increase in kcat for 3,4,5,6-inositol tetrakisphosphate compared to the wild type enzyme
H196A
the mutant shows reduced activity compared to the wild type enzyme
K168A
K200A
the mutant shows reduced activity compared to the wild type enzyme
N238A
the mutant shows reduced activity compared to the wild type enzyme
N239A
the mutant shows reduced activity compared to the wild type enzyme
R192A
the mutant shows reduced activity compared to the wild type enzyme
R415A
the mutant shows reduced activity compared to the wild type enzyme
R45A
the mutant shows reduced activity compared to the wild type enzyme
Y419A
the mutant shows reduced activity compared to the wild type enzyme
Q64A/E66A/E67A
D437A
site-directed mutagenesis, the mutant enzyme shows highly reduced activity
K138A
site-directed mutagenesis, the mutant enzyme shows highly reduced activity
additional information
D368A
site-directed mutagenesis, mutant IPK1D368A shows loss of kinase activity in vitro
K168A
site-directed mutagenesis, mutant IPK1K168AD shows loss of kinase activity in vitro
Q64A/E66A/E67A
site-directed mutagenesis, mutant structure analysis with bound reaction products IP6 and ADP. CnIpk1 mutant Q64A/E66A/E67A forms a crystal but only in the presence of the products IP6 and ADP
Q64A/E66A/E67A
Cryptococcus neoformans var. grubii ATCC 208821
-
site-directed mutagenesis, mutant structure analysis with bound reaction products IP6 and ADP. CnIpk1 mutant Q64A/E66A/E67A forms a crystal but only in the presence of the products IP6 and ADP
-
Q64A/E66A/E67A
Cryptococcus neoformans var. grubii CBS 10515
-
site-directed mutagenesis, mutant structure analysis with bound reaction products IP6 and ADP. CnIpk1 mutant Q64A/E66A/E67A forms a crystal but only in the presence of the products IP6 and ADP
-
Q64A/E66A/E67A
Cryptococcus neoformans var. grubii FGSC 9487
-
site-directed mutagenesis, mutant structure analysis with bound reaction products IP6 and ADP. CnIpk1 mutant Q64A/E66A/E67A forms a crystal but only in the presence of the products IP6 and ADP
-
additional information
generation of ipk1-1 mutants, phenotype, overview. Genetic interaction analysis of ITPK1 (EC 2.7.1.134) and IPK1 (EC 2.7.1.158) with a genetic cross between ipk1-1 and itpk1 mutants. The ipk1-1 itpk1 double mutants exhibit more severe growth defects than single mutants and those that, proceeded to the reproductive stage, bore aborted seeds. Common elevation of D/L-Ins(3,4,5,6)P4 in itpk1 and ipk1-1 mutants
additional information
-
generation of ipk1-1 mutants, phenotype, overview. Genetic interaction analysis of ITPK1 (EC 2.7.1.134) and IPK1 (EC 2.7.1.158) with a genetic cross between ipk1-1 and itpk1 mutants. The ipk1-1 itpk1 double mutants exhibit more severe growth defects than single mutants and those that, proceeded to the reproductive stage, bore aborted seeds. Common elevation of D/L-Ins(3,4,5,6)P4 in itpk1 and ipk1-1 mutants
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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.
the first bound Zn2+ ion, Zn1, is necessary for protein folding and stability
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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.
by batch-elution from Ni-NTA affinity resin, Analysis by SDS-PAGE gel and Western Blot using an anti-His antibody. Purity of protein is >98% estimated by SDS-PAGE.
recombinant
recombinant His-tagged enzyme from Escherichia coli strain BL21 (Lys) DE3 by nickel affinity chromatography
recombinant LSLt-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by heparin affinity chromatography and gel filtration followed by tag cleavage with TEV protease and again heparin affinity chromatography and gel filtration. The recombinant GST-tagged enzyme from Sf21 insect cells is purified by glutathione affinity chromatography and tag cleavage with PreScission protease, followed by heparin affinity chromatography and gel filtration
recombinant N-terminally His5-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and tag cleavage through TEV protease, followed by another step of nickel affinity chromatography, and gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cloning from a potato tuber cDNA library and expression of StITPK1-His protein in Escherichia coli rosetta cells.
expression in Escherichia coli
expression in Sf21 cells. Expression of the human enzyme in yeast ipk null strain restores synthesis of 1D-myo-inositol hexakisphosphate and rescues the gle1-2 ipk1-4 lethal phenotype
-
gene Glyma04g03240, sequence comaprisons and phylogenetic tree, quantitative real-time expression analysis
gene Glyma06g03310, sequence comaprisons and phylogenetic tree, quantitative real-time expression analysis
gene GmIpk1, sequence comparisons and phylogenetic tree, quantitative real-time expression analysis
gene IPK1, DNA and amio acid sequence determination and analysis, sequence comparisons and phylogenetic tree, quantitative real-time PCR enzyme expression analysis
gene ipk1, recombinant expression of LSLt-tagged enzyme in Escherichia coli strain BL21 Star (DE3), and recombinant expression of GST-tagged enzyme in Spodoptera frugiperda Sf21 cells. LSLt is a fragment of Laetiporus sulphurous lectin
gene IPK1, recombinant expression of N-terminally His5-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (Lys) DE3
spIpk1 functionally complements ipk1 mutants of Saccharomyces cerevisiae
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
assessing early kidney structural damage in diabetic kidney disease (DKD) via a urine biomarker is an appealing goal, and IPP2K may be a promising candidate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
York, J.D.; Odom, A.R.; Murphy, R.; Ives, E.B.; Wente, S.R.
A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
Science
285
96-100
1999
Saccharomyces cerevisiae
brenda
Ongusaga, P.P.; Hughes, P.J.; Davey, J.; Michell, R.H.
Inositol hexakisphosphate in Schizosaccharomyces pombe: synthesis from Ins(1,4,5)P3 and osmotic regulation
Biochem. J.
335
671-679
1998
Schizosaccharomyces pombe
-
brenda
Sweetman, D.; Johnson, S.; Caddick, S.E.; Hanke, D.E.; Brearley, C.A.
Characterization of an Arabidopsis inositol 1,3,4,5,6-pentakisphosphate 2-kinase (AtIPK1)
Biochem. J.
394
95-103
2006
Arabidopsis thaliana
brenda
Phillippy, B.Q.; Ullah, A.H.J.; Ehrlich, K.C.
Purification and some properties of inositol 1,3,4,5,6-pentakis phosphate 2-kinase from immature soybean seeds
J. Biol. Chem.
269
28393-28399
1994
Glycine max
brenda
Ives, E.B.; Nichols, J.; Wente, S.R.; York, J.D.
Biochemical and functional characterization of inositol 1,3,4,5,6-pentakisphosphate 2-kinases
J. Biol. Chem.
275
36575-36583
2000
Saccharomyces cerevisiae, Schizosaccharomyces pombe (Q9USK0), Schizosaccharomyces pombe
brenda
Verbsky, J.W.; Wilson, M.P.; Kisseleva, M.V.; Majerus, P.W.; Wente, S.R.
The synthesis of inositol hexakisphosphate. Characterization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
J. Biol. Chem.
277
31857-31862
2002
Homo sapiens
brenda
Miller, A.L.; Suntharalingam, N.; et al.
Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway
J. Biol. Chem.
279
51022-51032
2004
Saccharomyces cerevisiae
brenda
Fujii, M.; York, J.D.
A role for rat inositol polyphosphate kinases rIPK2 and rIPK1 in inositol pentakisphosphate and inositol hexakisphosphate production in rat-1 cells
J. Biol. Chem.
280
1156-1164
2005
Rattus norvegicus, Rattus norvegicus (Q5PXE9)
brenda
Verbsky, J.; Lavine, K.; Majerus, P.W.
Disruption of the mouse inositol 1,3,4,5,6-pentakisphosphate 2-kinase gene, associated lethality, and tissue distribution of 2-kinase expression
Proc. Natl. Acad. Sci. USA
102
8448-8453
2005
Mus musculus
brenda
Brehm, M.A.; Schenk, T.M.; Zhou, X.; Fanick, W.; Lin, H.; Windhorst, S.; Nalaskowski, M.M.; Kobras, M.; Shears, S.B.; Mayr, G.W.
Intracellular localization of human inositol 1,3,4,5,6-pentakisphosphate 2-kinase
Biochem. J.
408
335-345
2007
Homo sapiens
brenda
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
Plant Physiol.
144
1278-1291
2007
Zea mays, Zea mays (A4GWX8), Zea mays (A6YH13)
brenda
Caddick, S.E.; Harrison, C.J.; Stavridou, I.; Mitchell, J.L.; Hemmings, A.M.; Brearley, C.A.
A Solanum tuberosum inositol phosphate kinase (StITPK1) displaying inositol phosphate-inositol phosphate and inositol phosphate-ADP phosphotransferase activities
FEBS Lett.
582
1731-1737
2008
Solanum tuberosum (A4H2J0), Solanum tuberosum
brenda
Sarmah, B.; Wente, S.R.
Dual functions for the Schizosaccharomyces pombe inositol kinase Ipk1 in nuclear mRNA export and polarized cell growth
Eukaryot. Cell
8
134-146
2009
Schizosaccharomyces pombe (Q9USK0), Schizosaccharomyces pombe
brenda
Poehlmann, J.; Fleig, U.
Asp1, a conserved 1/3 inositol polyphosphate kinase, regulates the dimorphic switch in Schizosaccharomyces pombe
Mol. Cell. Biol.
30
4535-4547
2010
Schizosaccharomyces pombe
brenda
Wundenberg, T.; Grabinski, N.; Lin, H.; Mayr, G.W.
Discovery of InsP6-kinases as InsP6-dephosphorylating enzymes provides a new mechanism of cytosolic InsP6 degradation driven by the cellular ATP/ADP ratio
Biochem. J.
462
173-184
2014
Homo sapiens, Rattus norvegicus
brenda
Chanduri, M.; Rai, A.; Malla, A.B.; Wu, M.; Fiedler, D.; Mallik, R.; Bhandari, R.
Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport
Biochem. J.
473
3031-3047
2016
Mus musculus (Q6PD10)
brenda
Wang, H.; Godage, H.Y.; Riley, A.M.; Weaver, J.D.; Shears, S.B.; Potter, B.V.
Synthetic inositol phosphate analogs reveal that PPIP5K2 has a surface-mounted substrate capture site that is a target for drug discovery
Chem. Biol.
21
689-699
2014
Homo sapiens
brenda
Gosein, V.; Miller, G.J.
Roles of phosphate recognition in inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) substrate binding and activation
J. Biol. Chem.
288
26908-26913
2013
Arabidopsis thaliana (Q93YN9)
brenda
Gosein, V.; Miller, G.J.
Conformational stability of inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPK1) dictates its substrate selectivity
J. Biol. Chem.
288
36788-36795
2013
Arabidopsis thaliana
brenda
Brehm, M.; Wundenberg, T.; Williams, J.; Mayr, G.; Shears, S.
A non-catalytic role for inositol 1,3,4,5,6-pentakisphosphate 2-kinase in the synthesis of ribosomal RNA
J. Cell Sci.
126
437-444
2013
Homo sapiens
-
brenda
Sun, Y.Y.; Xu, W.Z.; Wu, L.; Wang, R.Z.; He, Z.Y.; Ma, M.
An Arabidopsis mutant of inositol pentakisphosphate 2-kinase AtIPK1 displays reduced arsenate tolerance
Plant Cell Environ.
39
416-426
2016
Arabidopsis thaliana (Q93YN9), Arabidopsis thaliana
brenda
Kuo, H.F.; Chang, T.Y.; Chiang, S.F.; Wang, W.D.; Charng, Y.Y.; Chiou, T.J.
Arabidopsis inositol pentakisphosphate 2-kinase, AtIPK1, is required for growth and modulates phosphate homeostasis at the transcriptional level
Plant J.
80
503-515
2014
Arabidopsis thaliana (Q93YN9)
brenda
Yu, J.; Saiardi, A.; Greenwood, J.S.; Bewley, J.D.
Molecular and biochemical identification of inositol 1,3,4,5,6-pentakisphosphate 2-kinase encoding mRNA variants in castor bean (Ricinus communis L.) seeds
Planta
239
965-977
2014
Ricinus communis
brenda
Basak, N.; Krishnan, V.; Pandey, V.; Punjabi, M.; Hada, A.; Marathe, A.; Jolly, M.; Palaka, B.K.; Ampasala, D.R.; Sachdev, A.
Expression profiling and in silico homology modeling of inositol pentakisphosphate 2-kinase, a potential candidate gene for low phytate trait in soybean
3 Biotech
10
268
2020
Glycine max (I1JT87), Glycine max (U5TRK1), Glycine max
brenda
Looker, H.C.; Merchant, M.L.; Rane, M.J.; Nelson, R.G.; Kimmel, P.L.; Rovin, B.H.; Klein, J.B.; Mauer, M.; Mauer, M.
Urine inositol pentakisphosphate 2-kinase and changes in kidney structure in early diabetic kidney disease in type 1 diabetes
Am. J. Physiol. Renal Physiol.
315
F1484-F1492
2018
Homo sapiens (Q9H8X2), Homo sapiens
brenda
Whitfield, H.; White, G.; Sprigg, C.; Riley, A.M.; Potter, B.V.L.; Hemmings, A.M.; Brearley, C.A.
An ATP-responsive metabolic cassette comprised of inositol tris/tetrakisphosphate kinase 1 (ITPK1) and inositol pentakisphosphate 2-kinase (IPK1) buffers diphosphosphoinositol phosphate levels
Biochem. J.
477
2621-2638
2020
Arabidopsis thaliana (Q93YN9)
brenda
Basak, N.; Krishnan, V.; Pandey, V.; Punjabi, M.; Hada, A.; Marathe, A.; Jolly, M.; Sachdev, A.
Molecular characterization of inositol pentakisphosphate 2-kinase (GmlPk1) from soybean and its expression pattern in the developing seeds
Indian J. Genet. Plant Breed.
77
371-378
2017
Glycine max (U5TRK1)
-
brenda
Franco-Echevarria, E.; Sanz-Aparicio, J.; Brearley, C.A.; Gonzalez-Rubio, J.M.; Gonzalez, B.
The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function
J. Biol. Chem.
292
10534-10548
2017
Mus musculus (Q6P1C1), Mus musculus
brenda
Whitfield, H.; Gilmartin, M.; Baker, K.; Riley, A.M.; Godage, H.Y.; Potter, B.V.L.; Hemmings, A.M.; Brearley, C.A.
A fluorescent probe identifies active site ligands of inositol pentakisphosphate 2-kinase
J. Med. Chem.
61
8838-8846
2018
Arabidopsis thaliana (Q93YN9)
brenda
Oh, J.; Lee, D.G.; Bahn, Y.S.; Rhee, S.
Crystal structure of inositol 1,3,4,5,6-pentakisphosphate 2-kinase from Cryptococcus neoformans
J. Struct. Biol.
200
118-123
2017
Cryptococcus neoformans var. grubii (J9VKS8), Cryptococcus neoformans var. grubii FGSC 9487 (J9VKS8), Cryptococcus neoformans var. grubii ATCC 208821 (J9VKS8), Cryptococcus neoformans var. grubii CBS 10515 (J9VKS8)
brenda
Kuo, H.; Hsu, Y.; Lin, W.; Chen, K.; Munnik, T.; Brearley, C.; Chiou, T.
Arabidopsis inositol phosphate kinases IPK1 and ITPK1 constitute a metabolic pathway in maintaining phosphate homeostasis
Plant J.
95
613-630
2018
Arabidopsis thaliana (Q93YN9), Arabidopsis thaliana
brenda
Franco-Echevarria, E.; Sanz-Aparicio, J.; Troffer-Charlier, N.; Poterszman, A.; Gonzalez, B.
Crystallization and preliminary X-ray diffraction analysis of a mammal inositol 1,3,4,5,6-pentakisphosphate 2-kinase
Protein J.
36
240-248
2017
Mus musculus (Q6P1C1), Mus musculus
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.1.158)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
