Any feedback?
Information on EC 2.7.9.1 - pyruvate, phosphate dikinase and Organism(s) Zea mays and UniProt Accession P11155
for references in articles please use BRENDA:EC2.7.9.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.9.1 pyruvate, phosphate dikinaseSpecify your search results
Word Map
- 2.7.9.1
- phosphoenolpyruvate
- carboxylase
- maize
- pep
- mesophyll
-
nadp-malic
-
carboxykinase
- rubisco
- ribulose-1,5-bisphosphate
- nadp-me
- symbiosum
- flaveria
-
crassulacean
-
kranz
- glycosomal
-
adp-dependent
-
1,5-bisphosphate
-
pyrophosphorylated
- brownii
-
4.1.1.31
- pepcase
-
c4-like
- trinervia
-
swiveling
- miscanthus
- crystallinum
- drug development
- diagnostics
- pharmacology
- analysis
- agriculture
-
c4-type
- mesembryanthemum
The taxonomic range for the selected organisms is: Zea mays
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pyruvate orthophosphate dikinase, pyruvate phosphate dikinase, pyruvate pi dikinase, ppdk1, pyruvate-phosphate dikinase, c4-ppdk, osppdkb, ppdk2, cytosolic pyruvate orthophosphate dikinase, cyppdk, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PPDK
pyruvate orthophosphate dikinase
pyruvate, orthophosphate dikinase
pyruvate, Pi dikinase
-
-
-
-
pyruvate-inorganic phosphate dikinase
-
-
-
-
pyruvate-phosphate dikinase
-
-
-
-
pyruvate-phosphate dikinase (phosphorylating)
-
-
-
-
pyruvate-phosphate ligase
-
-
-
-
pyruvic-phosphate dikinase
-
-
-
-
pyruvic-phosphate ligase
-
-
-
-
PPDK
-
-
-
-
PPDK
-
-
pyruvate, orthophosphate dikinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pyruvate, phosphate phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9027-40-1
-
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
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
C4 acid cycle enzyme
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
rate-limiting enzyme of C4 acid cycle
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
C4 photosynthesis, late-stage accumulation of PPDK supports involvement in the starch-protein balance through restriction of ADP-glucose synthesis in dependence of diphosphate, role by influencing the balance of alanine-aromatic amino acid synthesis
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
-
-
?
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
the Opaque-2 gene has regulatory function in metabolic pathways, mutation of Opaque-2 affects PPDK activity, overview
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
activity with UTP, GTP and CTP is 1-3% of the activity with ATP
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
HPO42- is the substrate
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
activity strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
loses activity below about 12°C by dissociation of the tetramer, considered as one possible cause of the reduction of the photosynthetic rate of maize at low temperatures
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
different substrate concentrations for PPDK inhibition assay, pyruvate (40, 80, 160, 320, 480, and 720 micromol), ATP (20, 40, 60, 120, 240, and 480 micromol), and phosphate (0.3, 0.6, 1.2, 1.8, 2.7, and 4.32 mM)
-
-
r
additional information
?
-
-
involved in C4 dicarboxylic acid pathway in plant
-
-
?
additional information
?
-
-
differing functions of PPDK in C4 versus C3 plants, C4 PPDK regulatory proteins are involved in regulation of PPDK, mechanism, overview
-
-
?
additional information
?
-
-
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview
-
-
?
additional information
?
-
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview
-
-
?
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
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
C4 acid cycle enzyme
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
rate-limiting enzyme of C4 acid cycle
-
-
?
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
C4 photosynthesis, late-stage accumulation of PPDK supports involvement in the starch-protein balance through restriction of ADP-glucose synthesis in dependence of diphosphate, role by influencing the balance of alanine-aromatic amino acid synthesis
-
-
r
AMP + phosphoenolpyruvate + diphosphate
ATP + pyruvate + phosphate
-
the Opaque-2 gene has regulatory function in metabolic pathways, mutation of Opaque-2 affects PPDK activity, overview
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
-
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
activity strictly and reversibly regulated by light
-
r
ATP + pyruvate + phosphate
AMP + phosphoenolpyruvate + diphosphate
-
loses activity below about 12°C by dissociation of the tetramer, considered as one possible cause of the reduction of the photosynthetic rate of maize at low temperatures
-
-
?
additional information
?
-
-
involved in C4 dicarboxylic acid pathway in plant
-
-
?
additional information
?
-
-
differing functions of PPDK in C4 versus C3 plants, C4 PPDK regulatory proteins are involved in regulation of PPDK, mechanism, overview
-
-
?
additional information
?
-
-
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview
-
-
?
additional information
?
-
specific late-stage accumulation of the pyruvate orthophosphate dikinase, it plays a critical rolein the starch-protein balance through inorganic pyrophosphate-dependent restriction of ADP-glucose synthesis in addition to its usually reported influence on the alanine-aromatic amino acid synthesis balance, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
NH4+
NH4+
-
at saturated concentration of NH4Cl pyruvate formation activity is increased 20fold
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ilimaquinone
uncompetitive/mixed type versus pyruvate and versus ATP, 48% inhibition of C4 acid cycle evolution. IC50: 0.292 mM
PPDK regulatory protein
RP catalyzes reversible phosphorylation on T456 by RP, inactive form phoshorylated at T456, ADP-dependent, a catalytic His-phophorylation precedes phosphorylation at T456, pyruvate (2 mM) can inhibit inactivation by RP
-
ilimaquinone
-
selectively toxic to C4 plants, isolated from a marine sponge, heterocyclic compound, 3 rings, 2-D structure shown
unguinol
-
mixed noncompetitive inhibition of PPDK with respect to the substrates pyruvate and ATP, uncompetitive with respect to phosphate, phytotoxic effects (bleaching) on C4 plants, no effect on a model C3 plant (Hordeum vulgare)
unguinol
-
from fungal isolate F3000054, a mixed noncompetitive inhibitor of PPDK with respect to the substrates pyruvate and ATP and an uncompetitive inhibitor of PPDK with respect to phosphate. Unguinol has deleterious effects on a model C4 plant but no effect on a model C3 plant, effects in vivo, overview
additional information
rapid screening method to detect specific inhibitors of pyruvate phosphate dikinase. Organic extracts of about 6500 marine macroscopic organisms are tested for inhibition. Approximately 70% of the PPDK selective extracts are from sponges (phylum Porifera). The remaining 30% of active extracts that preferentially inhibit PPDK include ascidians, cnidarians, echinoderms, mollusks, and red algae, with 25% of these preferentially inhibiting PPDK
-
additional information
ADP-dependent inactivation assay of purified PPDK by bacterially-expressed RP described (47% inhibition of PPDK after 10min in presence of 2 mM ADP at 25°C), reversibility of RP activity by diphosphate-dependent reactivation assay described (1 mM diphosphate, at 25°C), SDS-PAGE and Western-Blot for detection of T456P-PPDK and RP
-
additional information
-
ADP-dependent inactivation assay of purified PPDK by bacterially-expressed RP described (47% inhibition of PPDK after 10min in presence of 2 mM ADP at 25°C), reversibility of RP activity by diphosphate-dependent reactivation assay described (1 mM diphosphate, at 25°C), SDS-PAGE and Western-Blot for detection of T456P-PPDK and RP
-
additional information
-
for PPDK inhibition assay 5 and 10 micrograms per ml of unguinol tested in the presence of different substrate concentrations, whole-plant phytotoxicity test (C4, C3),antimicrobial assays and anti-tumor cell assays described for unguinol, 2-D structure shown for further potential candidates to inhibit PPDK that are analogues of unguinol as acarogobien A, acarogobien B and guisinol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
like the native PPDK of maize the activity of the cold-tolerant recombinant enzyme construct is regulated by the PPDK regulatory protein RP
-
additional information
the protein kinase/phosphatase RP catalyzes reversibly phosphorylation of T456, active form dephosphorylated at T456, diphosphate-forming dephosphorylation mechanism, assay at 25°C
-
additional information
-
the protein kinase/phosphatase RP catalyzes reversibly phosphorylation of T456, active form dephosphorylated at T456, diphosphate-forming dephosphorylation mechanism, assay at 25°C
-
additional information
PPDK is light-activated, activation kinetics at different temperatures, overview
-
additional information
-
PPDK is light-activated, activation kinetics at different temperatures, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics at different temperature, the t1/2 for dephosphorylation of PPDK from chilling-acclimated Miscanthus x giganteus leaves increased to 3.1fold compared to warm-grown leaves, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.292
ilimaquinone
Zea mays
uncompetitive/mixed type versus pyruvate and versus ATP, 48% inhibition of C4 acid cycle evolution. IC50: 0.292 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1 - 0.19
-
leaf enzyme extract, pH and temperature not specified in the publication
additional information
specific activity of PPDK in plants transformed with the construct showing 17 amino acid substitutions inversely correlates with amount of enzyme in leaves, PPDK activity becomes constant when the amount is above 5 mg/g fresh weight, enzyme contents estimated by Western blot, spectrometric assay at 25°C, two transformants retained 70% of activity after 180 min indicating a comparable cold-tolerance like Flaveria brownii plants, further effect of cold-tolerant PPDK on photosynthetic rate estimated by measurement of CO2 uptake at leaf temperatures of 30°C, 20°C, 13°C, and 8°C, increase by 23% at 8°C shown, no effects at higher temperatures
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3
-
the competency of the enzyme in catalyzing its phosphoenolpyruvate-forming reaction at pH 7.0 is dramatically reduced, having only 6% of the rate at pH 8.3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
cold tolerance of recombinant maize plants estimated, crude leaf extracts placed on ice to measure residual PPDK activities, PPDK extracted from untransformed maize looses 90% of its activity after 20 min, a retained PPDK activity 70% of after 180 min in two transformants corresponds to a cold-tolerance shown for Flaveria brownii plants
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
annotation of different isoforms of one of the two cytosolic isoforms of PPDK of maize
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
time course analysis of seven developmental stages of maize, 4-40 days after pollination, significant PPDK accumulation at 21 days after pollination
pdk1 specifies the abundant mesophyll form of pyruvate phosphate dikinase
additional information
maize inbred line A188, recombinant cold tolerant PPDK protein, 3'-part of Flaveria brownii (Asteraceae) PPDK fused to maize PPDK, exon-intron boundaries unaffected, in one of the constructs 17 amino acid positions altered, amounts of recombinant PPDK estimated by western blot and densitometry calculated on the basis of leaf fresh weight, wide range among individual plants
proteomic study of maize endosperm development, PPDK is important, overview
-
transcriptomic, proteomic and metabolic analysis of maize endosperm development, PPDK is important, overview
pdk2 accounts for the large majority of endosperm pyruvate phosphate dikinase
additional information
enzyme activity at different climates, cold climates at 14°C and warm climates at 25°C, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
seven isoforms of cytosolic PPDK of maize identified by proteomics, distinguished by deduced molecular mass, isoelectric point and slight differences in primary peptide sequence, in silico prediction of subcellular destination
the mature isozyme CyPPDKZm1 contains the 11-residue sequence MAPAPCGRSSQ
high levels of PPDK protein accumulate in mesophyll chloroplasts, identification of a transit peptide cleavage site, the mature isozyme C4PPDK contains the specific N-terminal sequence TTKK
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
evolution
-
three-dimensional modeling of PPDKs from divergent organisms and comparion of the orientation of the phosphorylatable histidine residue within the central domain of PPDKs. These PPDKs are compared using a maximum-likelihood tree. Phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
malfunction
metabolism
physiological function
additional information
-
role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis
malfunction
an opaque phenotype results complete pyruvate phosphate dikinase knockout, including loss of vitreous endosperm character
malfunction
the pdk1- mutation is seedling-lethal, indicating that C4 photosynthesis is essential in maize
physiological function
PPDK is the key enzyme of the C4 pathway, and its activity may limit the photosynthesis rate in maize leaves. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is strictly controlled by light intensity. Diverse regulatory pathways may work alone or in combination to fine-tune C4PPDK activity in response to changes in light
physiological function
pyruvate phosphate dikinase modulates endosperm metabolism, potentially through reversible adjustments to energy charge
malfunction
an opaque phenotype results complete pyruvate phosphate dikinase knockout, including loss of vitreous endosperm character
malfunction
-
the maize transposable elements Mutator and Ds are used to generate multiple mutant alleles of pyruvate orthophosphate dikinase (PPDK). Loss-of-function mutants are seedling lethal, even when plants are grown under 2% CO2, and they show very low capacity for CO2 assimilation, indicating C4 photosynthesis is essential in maize. Loss of PPDK results in downregulation of gene expression of enzymes of theC4 cycle, the Calvin cycle, and components of photochemistry. The loss of PPDK does not change Kranz anatomy, indicating that this metabolic defect in the C4 cycle does not impinge on the morphological differentiation of C4 characters. However, sugar metabolism and nitrogen utilization are altered in the mutants
metabolism
-
the enzyme plays a controlling role in the phosphoenolpyruvate-regeneration phase of the C4 photosynthetic pathway
metabolism
-
in C4 photosynthesis, pyruvate orthophosphate dikinase catalyzes the regeneration of phosphoenolpyruvate in the carbon shuttle pathway
physiological function
-
C4-PPDK expression in rice promotes nitrogen absorption from the soil. In addition, the photosynthesis rate of some transgenic IR64 lines is also increased in the greenhouse
physiological function
PPDK is the key enzyme of the C4 pathway, and its activity may limit the photosynthesis rate in maize leaves. The amount of PPDK (unphosphorylated) involved in C4 photosynthesis is strictly controlled by light intensity
physiological function
-
PPDK regulatory protein (PDRP) regulates the phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation
physiological function
pyramiding expression of Zea mays genes encoding phosphoenolpyruvate carboxylase (PEPC) and pyruvate orthophosphate dikinase (PPDK) synergistically improve the photosynthetic characteristics of transgenic Triticum aestivum
physiological function
-
pyruvate phosphate dikinase reversibly catalyzes the interconversion of phosphoenolpyruvate and pyruvic acid, leading to catabolism and adenosine triphosphate (ATP) synthesis or gluconeogenesis and ATP consumption. The orientation of the phosphorylatable histidine residue within the central domain of PPDK determines whether this enzyme promotes catabolism or gluconeogenesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPDK1_MAIZE
947
0
102674
Swiss-Prot
Chloroplast (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
370000
94000
95000
additional information
95000
-
4 * 95000, dissociates into largely inactive dimers and tetramers when subjected to cold temperatures in vitro
95000
-
4 * 95000, the enzyme is maximally active as a homotetramer and is inactive in the dimeric and monomeric forms
additional information
-
different isoforms of one of the two cytosolic isoforms of PPDK of maize distinguished by pI value, molecular mass and altered amino acid positions in identified peptides by isoelectric focusing, 2-D electrophoresis and liquid chromatography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
-
4 * 95000, the enzyme is maximally active as a homotetramer and is inactive in the dimeric and monomeric forms
tetramer
additional information
-
role of the N- and C-termini on the orientation of the PPDK central domain, three-dimensional structure analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
additional information
phosphoprotein
phosphorylation/dephosphorylation by the PPDK regulatory protein RP at T456, RP-reaction described as PPDK-T456 + ADP = PPDK-T456P + AMP and PPDK-T456P + phophate = PPDK-T456 + diphosphate
phosphoprotein
in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site Thr residue, catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. Light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr527 of PPDK in Zea mays. PDRP catalyzes the reversible phosphorylation of PPDK rapidly and efficiently, but a subtle conformational change around PPDK's active site Thr527 will affect its catalytic efficiency. Phosphorylation at Thr527 of PPDK is independent of the light/dark transition. The plastidic isozyme shows phosphorylation at four serine (Ser)/Thr residues, Thr527, Ser528, Thr309, and Ser506 are targets of PDRP. The two hydrogen bonds between the highly conserved residues Ser528 and Gly525 are required for PDRP-mediated phosphorylation of the active-site Thr527 of the isozyme. Analysis by high resolution mass spectrometry, locations of the four phosphorylation residues in the primary sequence and the three-dimensional structure of C4PPDK, modelling, overview
phosphoprotein
-
PPDK activity in C4 chloroplasts is light-regulated via reversible phosphorylation of an active-site Thr residue by the PPDK regulatory protein, i.e. C4 RP, a most unusual bifunctional protein kinase /protein phosphatase, overview
phosphoprotein
-
the PPDK regulatory protein catalyses this light-dependent regulation of the enzyme by reversible phosphorylation of the active-site Thr456 residue
phosphoprotein
in C4 plants, pyruvate orthophosphate dikinase (PPDK) activity is tightly dark/light regulated by reversible phosphorylation of an active-site Thr residue, catalyzed by PPDK regulatory protein (PDRP). Phosphorylation and dephosphorylation of PPDK lead to its inactivation and activation, respectively. Light intensity rather than the light/dark transition regulates PPDK activity by modulating the reversible phosphorylation at Thr527 of PPDK in Zea mays. PDRP catalyzes the reversible phosphorylation of PPDK rapidly and efficiently, but a subtle conformational change around PPDK's active site Thr527 will affect its catalytic efficiency. Analysis by high-resolution mass spectrometry
phosphoprotein
-
reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein (PDRP) , structural analysis and molecular catalytic mechanism, overview. The homodimeric PPDK regulatory protein regulates the inorganic phosphate-dependent activation and ADP-dependent inactivation of PPDK by reversible phosphorylation. Residue Asp277 is used for protonating and deprotonating the target Thr residue of PPDK to promote nucleophilic attack
additional information
partial amino-terminal acetylation of the plastidic isozyme
additional information
partial amino-terminal acetylation of the plastidic isozyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, crystal strcuture with and without phosphoenolpyruvate, determined at 2.3 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G525A
site-directed mutagenesis, the mutant shows no phosphorylation signal
G525P
site-directed mutagenesis, the mutant shows no phosphorylation signal
S528C
site-directed mutagenesis, the mutant shows a phosphorylation signal only slightly weaker than the wild-type enzyme due to the tighter binding of S528 to G525 compared to C528
S528T
site-directed mutagenesis, the mutant shows no phosphorylation signal
S528Y
site-directed mutagenesis, the mutant shows no phosphorylation signal
T456F
T456Y
additional information
additional information
point mutations introduced into exons 15, 16, 17, 18, and 19 of the maize PPDK gene to generate a construct altered at 17 amino acid positions at the C-terminus that mimicks the 3'-part of PPDK of Flaveria brownii (Asteraceae) encoding the C-terminal part of PPDK responsible for cold tolerance, two other constructs represent a fusion protein of the 3'-part of PPDK of Flaveria brownii (Asteraceae) and maize PPDK, a further construct of maize PPDK serves as a control
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12
-
loses activity below at about 12°C by dissociation of the tetramer, considered as one possible cause of the reduction of the photosynthetic rate of maize at low temperatures
additional information
additional information
up to 70% of activity of PPDK retained after incubation of transformed leaf extracts for 180 min on ice, 5fold increased amounts of recombinant enzyme by using a construct with seventeen amino acid substitutions, PPDK extracted from untransformed maize lost 90% of its activity after 20 min, in recombinant plants the photosynthetic rate (CO2 uptake) at 8°C significantly increased by 23%, no obvious effect at higher temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native isozymes from leaves, subcellular fractionation, recombinant tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (RIL) by immobilized metal affinity chromatography
recombinant maize PPDK used for inactivation/activation assay by the PPDK regulatory protein RP
maize PPDK of leaves expressed for inhibitor studies in Escherichia coli with a His-tag and purified on a Ni-affinity column
-
method that includes successive chromatography through DE-52, hydroxyapatite, Sephadex G-200 and Blue agarose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli, three constructs, one construct consisting of the 3'-part of Flaveria brownii (Asteraceae) of cold tolerant PPDK fused to maize PPDK (15th exon), another construct includes a set of point mutations to substitute all of the 17 residues that differ between the 3'-parts of maize and Flaveria brownii PPDK, respectively, the whole genomic sequence of the maize PPDK gene is included as a control, transformation of constructs into maize inbred line A188 by Agrobacterium tumefaciens (strain LBA4404), individual range of variation in the amount of PPDK among regenerated plants, crude leaf extracts of some transformed plants produce a large amount of cold tolerant recombinant enzyme and reveal a greatly improved cold tolerance especially by using the construct altered at 17 amino acid positions
gene C4ppdkZm1, quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (RIL)
quantitative real-time reverse transcription (RT)-PCR expression analysis during transfer of plants from 25°C to 14°C growth temperature
expressed in Arabidopsis thaliana, found exclusively in chloroplasts of transgenic Arabidopsis plants
-
gene PPDK, phylogenetic analysis of the N- and C-terminal sequences of PPDKs from different species, overview
-
gene ppdk, Triticum aestivum cv. Zhoumai19 immature embryosare transfected by particle bombardment with chimeric genes containing pepc or ppdk cDNA and the bialaphos resistance gene under the control of the Cauliflower mosaic virus 35S promoter. Three types of transgenic lines containing 1. pepc cDNA (PC lines), 2. ppdk cDNA (PK lines), or 3. both genes (PKC lines) are obtained through callus differentiation, phosphinthricine resistance screening, plantlet regeneration, and molecular detection. Quantitative real-time PCR enzyme expression analysis. Net photosynthetic rates of mutants are increased compared to controls
quantitative expression analysis of the enzyme during endosperm development, expression profiles, overview
to improve the cold stability of the enzyme, a cold-tolerant PPDK cDNA isolated from Flaveria brownii is introduced into maize by Agrobacterium-mediated transformation. Higher levels of expression are ontained by using a double intron cassette and a chimeric cDNA made from Flaveria bidentis and Flaveria brownii with a maximum content of 1 mg/g fresh weight. In leaves of transgenic maize, PPDK molecules produced from the transgene are detected in cold-tolerant homotetramers or in heterotetramers of intermediate cold susceptibility formed with the internal PPDK. A significant improvement in the cold stability of PPDK can be achieved when a suffcient quantity of cold-tolerant subunits is expressed in transgenic maize leaves
-
quantitative expression analysis of the enzyme during endosperm development, expression profiles, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
to improve the cold stability of the PPDK enzyme, studies on cold tolerance in plants
agriculture
-
modification of the cold sensitivity of a C4 photosynthetic enzyme by employing cereal transformation technology. A significant improvement in the cold stability of PPDK can be achieved when a suffcient quantity of cold-tolerant subunits is expressed in transgenic maize leaves
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakamoto, H.; Edwards, G.E.
Effect of magnesium, manganese and phosphate on catalysis of pyruvate, orthophosphate dikinase from maize
Plant Physiol. Biochem.
28
553-559
1990
Zea mays
-
Salahas, G.; Manetas, Y.; Gavalas, N.A.
Effects of glycerol on in vitro stability and regulatory activation /inactivation of pyruvate, orthophosphate dikinase of Zea mays
Photosynth. Res.
26
9-17
1990
Zea mays
Hatch, M.D.; Slack, C.R.
Pyruvate, Pi dikinase from leaves
Methods Enzymol.
42C
212-219
1975
Arundinaria sp., Zea mays
-
Sugiyama, T.
Purification, molecular, and catalytic properties of pyruvate phosphate dikinase from the maize leaf
Biochemistry
12
2862-2868
1973
Zea mays
Shirahashi, K.; Hayakawa, S.; Sugiyama, T.
Cold lability of pyruvate, orthophosphate dikinase in the maize leaf
Plant Physiol.
62
826-830
1978
Zea mays
Jenkins, C.L.D.; Hatch, M.D.
Properties and reaction mechanism of C4 leaf pyruvate,Pi dikinase
Arch. Biochem. Biophys.
239
53-62
1985
Zea mays
Sugiyama, T.; Iwaki, H.
Purification and partial characterization of inactive pyruvate orthophosphate dikinase from dark-treated maize leaves
Agric. Biol. Chem.
41
1239-1244
1977
Zea mays
-
Nakamoto, H.; Edwards, G.E.
Effect of adenine nucleotides on the reaction catalyzed by pyruvate,orthophosphate dikinase in maize
Biochim. Biophys. Acta
924
360-368
1987
Zea mays
-
Smith, C.M.; Duff, S.M.; Chollet, R.
Partial purification and characterization of maize-leaf pyruvate, orthophosphate dikinase regulatory protein: a low-abundance, mesophyll-chloroplast stromal protein
Arch. Biochem. Biophys.
308
200-206
1994
Zea mays
Usami, S.; Ohta, S.; Komari, T.; Burnell, J.N.
Cold stability of pyruvate, orthophosphate dikinase of Flaveria brownii
Plant Mol. Biol.
27
969-980
1995
Zea mays, Flaveria brownii (Q39734), Flaveria brownii, Flaveria bidentis (Q39735), Flaveria bidentis
Chastain, C.J.; Thompson, B.J.; Chollet, R.
Maize recombinant C4-pyruvate, orthophosphate dikinase: expression in Escherichia coli, partial purification, and characterization of the phosphorylatable protein
Photosynth. Res.
49
83-89
1996
Zea mays
Ishimaru, K.; Ichikawa, H.; Matsuoka, M.; Ohsugi, R.
Analysis of a C4 maize pyruvate, orthophosphate dikinase expressed in C3 transgenic Arabidopsis plants
Plant Sci.
129
57-64
1997
Zea mays
-
Ohta, S.; Usami, S.; Ueki, J.; Kumashiro, T.; Komari, T.; Burnell, J.N.
Identification of the amino acid residues responsible for cold tolerance in Flaveria brownii pyruvate,orthophosphate dikinase
FEBS Lett.
403
5-9
1997
Flaveria bidentis, Flaveria brownii, Zea mays
Chastain, C.J.; Botschner, M.; Harrington, G.E.; Thompson, B.J.; Mills, S.E.; Sarath, G.; Chollet, R.
Further analysis of maize C(4) pyruvate,orthophosphate dikinase phosphorylation by its bifunctional regulatory protein using selective substitutions of the regulatory Thr-456 and catalytic His-458 residues
Arch. Biochem. Biophys.
375
165-170
2000
Zea mays
Chastain, C.J.; Chollet, R.
Regulation of pyruvate, orthophosphate dikinase by ADP-/Pi-dependent reversible phosphorylation in C3 and C4 plants
Plant Physiol. Biochem.
41
523-532
2003
Zea mays
-
Nakanishi, T.; Nakatsu, T.; Matsuoka, M.; Sakata, K.; Kato, H.
Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion
Biochemistry
44
1136-1144
2005
Zea mays (P11155), Zea mays
Haines, D.S.; Burnell, J.N.; Doyle, J.R.; Llewellyn, L.E.; Motti, C.A.; Tapiolas, D.M.
Translation of in vitro inhibition by marine natural products of the C4 acid cycle enzyme pyruvate Pi dikinase to in vivo C4 plant tissue death
J. Agric. Food Chem.
53
3856-3862
2005
Zea mays (P11155)
Doyle, J.R.; Burnell, J.N.; Haines, D.S.; Llewellyn, L.E.; Motti, C.A.; Tapiolas, D.M.
A rapid screening method to detect specific inhibitors of pyruvate orthophosphate dikinase as leads for C4 plant-selective herbicides
J. Biomol. Screen.
10
67-75
2005
Zea mays (P11155)
Ohta, S.; Ishida, Y.; Usami, S.
Expression of cold-tolerant pyruvate, orthophosphate dikinase cDNA, and heterotetramer formation in transgenic maize plants
Transgenic Res.
13
475-485
2004
Flaveria bidentis, Flaveria brownii, Zea mays
Motti, C.A.; Bourne, D.G.; Burnell, J.N.; Doyle, J.R.; Haines, D.S.; Liptrot, C.H.; Llewellyn, L.E.; Ludke, S.; Muirhead, A.; Tapiolas, D.M.
Screening marine fungi for inhibitors of the C4 plant enzyme pyruvate phosphate dikinase: unguinol as a potential novel herbicide candidate
Appl. Environ. Microbiol.
73
1921-1927
2007
Zea mays
Burnell, J.N.; Chastain, C.J.
Cloning and expression of maize-leaf pyruvate, Pi dikinase regulatory protein gene
Biochem. Biophys. Res. Commun.
345
675-680
2006
Zea mays (P11155), Zea mays
Ohta, S.; Ishida, Y.; Usami, S.
High-level expression of cold-tolerant pyruvate, orthophosphate dikinase from a genomic clone with site-directed mutations in transgenic maize
Mol. Breed.
18
29-38
2006
Zea mays (P11155)
Mechin, V.; Thevenot, C.; Le Guilloux, M.; Prioul, J.L.; Damerval, C.
Developmental analysis of maize endosperm proteome suggests a pivotal role for pyruvate orthophosphate dikinase
Plant Physiol.
143
1203-1219
2007
Zea mays, Zea mays (P11155)
Prioul, J.L.; Mechin, V.; Damerval, C.
Molecular and biochemical mechanisms in maize endosperm development: The role of pyruvate-Pi-dikinase and Opaque-2 in the control of C/N ratio
C. R. Biol.
331
772-779
2008
Zea mays
Chastain, C.J.; Xu, W.; Parsley, K.; Sarath, G.; Hibberd, J.M.; Chollet, R.
The pyruvate, orthophosphate dikinase regulatory proteins of Arabidopsis possess a novel, unprecedented Ser/Thr protein kinase primary structure
Plant J.
53
854-863
2008
Arabidopsis thaliana, Zea mays
Wang, D.; Portis, A.R.; Moose, S.P.; Long, S.P.
Cool C4 photosynthesis: pyruvate pi dikinase expression and activity corresponds to the exceptional cold tolerance of carbon assimilation in Miscanthus x giganteus
Plant Physiol.
148
557-567
2008
Miscanthus x giganteus, Zea mays (P11155), Zea mays
Zhang, J.; Bandyopadhyay, A.; Sellappan, K.; Wang, G.; Xie, H.; Datta, K.; Datta, S.
Characterization of a C4 maize pyruvate orthophosphate dikinase expressed in C3 transgenic rice plants
Afr. J. Biotechnol.
9
234-242
2010
Zea mays
-
Chastain, C.J.; Failing, C.J.; Manandhar, L.; Zimmerman, M.A.; Lakner, M.M.; Nguyen, T.H.
Functional evolution of C4 pyruvate, orthophosphate dikinase
J. Exp. Bot.
62
3083-3091
2011
Zea mays
Feng, X.; Yang, C.; Zheng, W.; Wen, J.
Structural and evolutionary characteristics of pyruvate phosphate dikinase in Giardia lamblia and other amitochondriate protozoa
Chin. Med. Sci.
127
4097-4103
2014
Zea mays, Trypanosoma brucei (O76283), Giardia intestinalis (P51776), Giardia intestinalis
Famiani, F.; Paoletti, A.; Battistelli, A.; Moscatello, S.; Chen, Z.H.; Leegood, R.C.; Walker, R.P.
Phosphoenolpyruvate carboxykinase, pyruvate orthophosphate dikinase and isocitrate lyase in both tomato fruits and leaves, and in the flesh of peach and some other fruits
J. Plant Physiol.
202
34-44
2016
Capsicum annuum, Solanum lycopersicum, Zea mays, no activity in Prunus persica var. Adriatica, no activity in Solanum melongena var. Black Enorma, Hoya carnosa
Chen, Y.B.; Lu, T.C.; Wang, H.X.; Shen, J.; Bu, T.T.; Chao, Q.; Gao, Z.F.; Zhu, X.G.; Wang, Y.F.; Wang, B.C.
Posttranslational modification of maize chloroplast pyruvate orthophosphate dikinase reveals the precise regulatory mechanism of its enzymatic activity
Plant Physiol.
165
534-549
2014
Zea mays (P11155), Zea mays (Q42368), Zea mays
Jiang, L.; Chen, Y.B.; Zheng, J.; Chen, Z.; Liu, Y.; Tao, Y.; Wu, W.; Chen, Z.; Wang, B.C.
Structural basis of reversible phosphorylation by maize pyruvate orthophosphate dikinase regulatory protein
Plant Physiol.
170
732-741
2016
Zea mays
Zhang, H.; Xu, W.; Wang, H.; Hu, L.; Li, Y.; Qi, X.; Zhang, L.; Li, C.; Hua, X.
Pyramiding expression of maize genes encoding phosphoenolpyruvate carboxylase (PEPC) and pyruvate orthophosphate dikinase (PPDK) synergistically improve the photosynthetic characteristics of transgenic wheat
Protoplasma
251
1163-1173
2014
Zea mays (D3K3U9), Zea mays
Zhang, Y.; Giuliani, R.; Zhang, Y.; Zhang, Y.; Araujo, W.L.; Wang, B.; Liu, P.; Sun, Q.; Cousins, A.; Edwards, G.; Fernie, A.; Brutnell, T.P.; Li, P.
Characterization of maize leaf pyruvate orthophosphate dikinase using high throughput sequencing
J. Integr. Plant Biol.
60
670-690
2018
Zea mays
Lappe, R.R.; Baier, J.W.; Boehlein, S.K.; Huffman, R.; Lin, Q.; Wattebled, F.; Settles, A.M.; Hannah, L.C.; Borisjuk, L.; Rolletschek, H.; Stewart, J.D.; Scott, M.P.; Hennen-Bierwagen, T.A.; Myers, A.M.
Functions of maize genes encoding pyruvate phosphate dikinase in developing endosperm
Proc. Natl. Acad. Sci. USA
115
E24-E33
2018
Zea mays (P11155), Zea mays (Q42368), Zea mays
EXTERNAL LINKS (specific for EC-Number 2.7.9.1)
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)
Legal
Curated at
Member of
