Information on EC 2.5.1.112 - adenylate dimethylallyltransferase (ADP/ATP-dependent)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.112
-
RECOMMENDED NAME
GeneOntology No.
adenylate dimethylallyltransferase (ADP/ATP-dependent)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + ADP = diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
show the reaction diagram
(1)
-
-
-
dimethylallyl diphosphate + ATP = diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
show the reaction diagram
(2)
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Metabolic pathways
-
-
trans-zeatin biosynthesis
-
-
Zeatin biosynthesis
-
-
mevalonate metabolism
-
-
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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
cultivar B73
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ADP
diphosphate + trans-zeatin riboside 5'-diphosphate
show the reaction diagram
-
-
-
-
?
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ADP
trans-zeatin riboside phosphate + phosphate
show the reaction diagram
2.2% activity compared to dimethylallyl diphosphate and ADP
-
-
?
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ATP
trans-zeatin riboside phosphate + diphosphate
show the reaction diagram
1.4% activity compared to dimethylallyl diphosphate and ADP
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
show the reaction diagram
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
show the reaction diagram
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
show the reaction diagram
dimethylallyl diphosphate + CDP
?
show the reaction diagram
30% activity compared to ADP
-
-
?
dimethylallyl diphosphate + CTP
?
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + dADP
?
show the reaction diagram
50% activity compared to ADP
-
-
?
dimethylallyl diphosphate + dATP
?
show the reaction diagram
dimethylallyl diphosphate + diadenosine hexaphosphate
?
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + diadenosine pentaphosphate
?
show the reaction diagram
-
diadenosine pentaphosphate exhibits the highest binding affinity
-
-
?
dimethylallyl diphosphate + diadenosine tetraphosphate
?
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + diadenosine triphosphate
?
show the reaction diagram
-
diadenosine pentaphosphate exhibits the lowest binding affinity and specific activity compared to ATP
-
-
?
dimethylallyl diphosphate + GDP
?
show the reaction diagram
6.4% activity compared to ADP
-
-
?
dimethylallyl diphosphate + GTP
?
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + UTP
?
show the reaction diagram
-
-
-
?
geranyl diphosphate + ADP
?
show the reaction diagram
1.2% activity compared to dimethylallyl diphosphate and ADP
-
-
?
isopentenyl diphosphate + ADP
?
show the reaction diagram
0.3% activity compared to dimethylallyl diphosphate and ADP
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxy-3-methyl-2-(E)-butenyl diphosphate + ADP
diphosphate + trans-zeatin riboside 5'-diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
show the reaction diagram
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine phosphate
show the reaction diagram
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
show the reaction diagram
additional information
?
-
-
1-hydroxy-2-methyl-2-buten-4-yl 4-diphosphate is not a substrate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0193 - 0.0682
ADP
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
0.0162 - 0.018
ATP
0.0065 - 0.0374
dimethylallyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
ADP
0.008
AMP
Humulus lupulus
-
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
Humulus lupulus
-
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
0.027 - 0.035
dimethylallyl diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.344 - 1.238
ADP
13
0.0109
AMP
Humulus lupulus
-
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
30
1.34
ATP
Humulus lupulus
-
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
4
0.921 - 1.397
dimethylallyl diphosphate
157
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
strong expression in developing kernel
Manually annotated by BRENDA team
expression of isoform IPT3
Manually annotated by BRENDA team
predominant expression of isoform IPT1
Manually annotated by BRENDA team
predominant expression of isoform IPT7
Manually annotated by BRENDA team
immature seed, predominant expression of isoform IPT1; immature seed, predominant expression of isoform IPT4; immature seed, predominant expression of isoform IPT8
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35810
x * 35810, calculated from amino acid sequence
36693
-
x * 36693, calculated from amino acid sequence
37000
-
x * 37000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-chelate affinity column chromatography
Ni-NTA agarose column chromatography
-
Ni-NTA resin column chromatography and Mono Q column chromatography
Talon metal affinity column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli AD494(DE3)pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21-Star cells
-
expressed in Escherichia coli M15 cells
-
expressed in Escherichia coli M15[pREP4] cells
-
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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