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Enzyme Nomenclature
Information on EC 2.5.1.112 - adenylate dimethylallyltransferase (ADP/ATP-dependent)
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.5.1.112
-
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RECOMMENDED NAME
GeneOntology No.
adenylate dimethylallyltransferase (ADP/ATP-dependent)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + ADP = diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
(1)
-
-
-
dimethylallyl diphosphate + ATP = diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
(2)
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:ADP/ATP dimethylallyltransferase
Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP [1]. Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus [3], also have a lower activity with AMP (cf. EC 2.5.1.27, adenylate dimethylallyltransferase).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins; the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins; the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins; the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins; the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins; the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins; the ipt1357 quadruple mutant possesses severely decreased levels of isopentenyladenine and trans-zeatin , and their corresponding ribosides, ribotides, and glucosides, and is retarded in its growth. In contrast, these mutants possess increased levels of cis-zeatin-type cytokinins
metabolism
physiological function
metabolism
the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis; the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis; the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis; the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis; the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis; the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis; the enzyme isoforms are responsible for the bulk of isopentenyladenine- and trans-zeatin-type cytokinin synthesis
metabolism
-
the isopentenyltransferase reaction is the key rate-limiting step in cytokinin biosynthesis
physiological function
interference of auxin distribution disrupts the cytokinin response and ATP/ADP isopentenyltransferase IPT5 expression, affecting stem cell initiation and meristem formation. Auxin response factor ARF3 mediates the auxin response during de novo organ regeneration. Mutations in ARF3 cause ectopic cytokinin biosynthesis via the misexpression of IPT5, and this disrupts organ regeneration. ARF3 directly binds to the promoter of IPT5 and negatively regulates IPT5 expression
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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
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ADP
diphosphate + trans-zeatin riboside 5'-diphosphate
-
-
-
-
?
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ADP
trans-zeatin riboside phosphate + phosphate
2.2% activity compared to dimethylallyl diphosphate and ADP
-
-
?
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ATP
trans-zeatin riboside phosphate + diphosphate
1.4% activity compared to dimethylallyl diphosphate and ADP
-
-
?
dimethylallyl diphosphate + diadenosine pentaphosphate
?
-
diadenosine pentaphosphate exhibits the highest binding affinity
-
-
?
dimethylallyl diphosphate + diadenosine triphosphate
?
-
diadenosine pentaphosphate exhibits the lowest binding affinity and specific activity compared to ATP
-
-
?
geranyl diphosphate + ADP
?
1.2% activity compared to dimethylallyl diphosphate and ADP
-
-
?
isopentenyl diphosphate + ADP
?
0.3% activity compared to dimethylallyl diphosphate and ADP
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
100% activity
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
-
?
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
-
low activity with AMP
-
-
?
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
6.6% activity compared to ADP
-
-
?
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
-
low efficiency
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
highest activity with ATP
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
ATP is the best cosubstrate
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
the enzme favors ATP as its ligand
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
82% activity compared to ADP
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
-
-
-
?
dimethylallyl diphosphate + dATP
?
the enzyme shows preference for dATP over ADP and 80% activity with dATP compared to ATP
-
-
?
additional information
?
-
-
GMP, IMP, CMP, and UMP are not accepted as a substrate
-
-
-
additional information
?
-
no activity with farnesyl diphosphate, dAMP, CMP, GMP, IMP, IDP, UMP, UDP, FAD and NADH
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ADP
diphosphate + trans-zeatin riboside 5'-diphosphate
-
-
-
-
?
additional information
?
-
-
1-hydroxy-2-methyl-2-buten-4-yl 4-diphosphate is not a substrate
-
-
-
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
Q93WC9, Q94ID1, Q94ID2, Q94ID3, Q9C6L1, Q9LJL4, Q9SB60
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
Q93WC9, Q94ID1, Q94ID2, Q94ID3, Q9C6L1, Q9LJL4, Q9SB60
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
Q5GHF7
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
Q08ET4
100% activity
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
-
-
-
-
?
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
Q08ET4
6.6% activity compared to ADP
-
-
?
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
-
low efficiency
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
Q93WC9, Q94ID1, Q94ID2, Q94ID3, Q9C6L1, Q9LJL4, Q9SB60
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
Q93WC9, Q94ID1, Q94ID2, Q94ID3, Q9C6L1, Q9LJL4, Q9SB60
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
highest activity with ATP
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
-
ATP is the best cosubstrate
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
Q5GHF7
the enzme favors ATP as its ligand
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
Q08ET4
82% activity compared to ADP
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the enzyme is dependent on presence of divalent cation, and addition of 2 mM MnCl2 is 1.3times more effective than that of 10 mM MgCl2
Mn2+
the enzyme is dependent on presence of divalent cation, and addition of 2 mM MnCl2 is 1.3times more effective than that of 10 mM MgCl2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.759
AMP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.0193
ADP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.0193
ADP
in HEPES (20mM, pH 7.0; 150 mM NaCl, 3 mM dithiothreitol), at 25°C
0.0682
ADP
in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C
0.0162
ATP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.0162
ATP
in HEPES (20mM, pH 7.0; 150 mM NaCl, 3 mM dithiothreitol), at 25°C
0.018
ATP
-
in 25 mM Tris-HCl, pH 7.5, 10 mM MgCl2+, 5 mM 2-mercaptoethanol at 24°C
0.0065
dimethylallyl diphosphate
-
in 25 mM Tris-HCl, pH 7.5, 10 mM MgCl2+, 5 mM 2-mercaptoethanol at 24°C
0.0195
dimethylallyl diphosphate
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.0374
dimethylallyl diphosphate
in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
AMP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.022
ATP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.024
ADP
-
in 100 mM TrisHCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.024
ADP
in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C
0.027
dimethylallyl diphosphate
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.035
dimethylallyl diphosphate
in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0109
AMP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
1.34
ATP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.344
ADP
in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C
1.238
ADP
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
0.921
dimethylallyl diphosphate
in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C
1.397
dimethylallyl diphosphate
-
in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of isoform IPT3
predominant expression of isoform IPT1
predominant expression of isoform IPT7
immature seed, predominant expression of isoform IPT1; immature seed, predominant expression of isoform IPT4; immature seed, predominant expression of isoform IPT8
predominant expression of isoform IPT4; predominant expression of isoform IPT8
predominant expression of isoform IPT1; predominant expression of isoform IPT7
predominant expression of isoform IPT1; predominant expression of isoform IPT5; predominant expression of isoform IPT7
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with ATP, sitting drop vapor diffusion method, using 0.2 M ammonium tartrate and 20% (w/v) PEG 3350
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-chelate affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
auxin response factor ARF3 directly binds to the promoter of IPT5 and negatively regulates IPT5 expression
enzyme expression is developmentally regulated in kernel tissues and coincides with cytokinin accumulation. The expression gradually increases from 6 to 8 days after pollination (DAP), peaks at 8 DAP, and decreases gradually until 14 DAP before increasing again at later stages (15-34 DAP)
-
isoform IPT1 is down-regulated by the cytokinin 4-(indol-3-yl)butyric acid within 4 h; isoform IPT3 is down-regulated by the cytokinin 4-(indol-3-yl)butyric acid within 4 h; isoform IPT5 is down-regulated by the cytokinin 4-(indol-3-yl)butyric acid within 4 h; isoform IPT7 is down-regulated by the cytokinin 4-(indol-3-yl)butyric acid within 4 h
isoform IPT3 is rapidly induced by 1 h treatment with nitrate; isoform IPT5 is up-regulated by 4,4'-isopropylidenediphenol (bisphenol A) treatment for 4 h; isoform IPT7 is up-regulated by 4,4'-isopropylidenediphenol (bisphenol A) treatment for 4 h
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D49A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
F120A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
F157A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
F93A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
Q255A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
W159A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
Y153A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
Y170A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP; the mutant retains 84% of wild type activity
Y217A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
Y54A
the mutant almost completely loses the enzyme activity for the prenyl transfer from dimethylallyl diphosphate to ADP
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LINKS TO OTHER DATABASES (specific for EC-Number 2.5.1.112)
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