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Information on EC 2.5.1.112 - adenylate dimethylallyltransferase (ADP/ATP-dependent) and Organism(s) Humulus lupulus and UniProt Accession Q5GHF7

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EC Tree
IUBMB Comments
Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP . Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus , also have a lower activity with AMP (cf. EC 2.5.1.27, adenylate dimethylallyltransferase).
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This record set is specific for:
Humulus lupulus
UNIPROT: Q5GHF7
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The taxonomic range for the selected organisms is: Humulus lupulus
The enzyme appears in selected viruses and cellular organisms
Synonyms
atp/adp ipt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylate isopentenyltransferase
-
2-isopentenyl-diphosphate:ADP/ATP DELTA2-isopentenyltransferase
-
-
-
-
adenylate isopentenyltransferase
-
-
dimethylallyl diphosphate:ATP/ADP isopentenyltransferase
-
-
-
-
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).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
show the reaction diagram
the enzme favors ATP as its ligand
-
-
?
dimethylallyl diphosphate + CTP
?
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + dATP
?
show the reaction diagram
the enzyme shows preference for dATP over ADP and 80% activity with dATP compared to ATP
-
-
?
dimethylallyl diphosphate + GTP
?
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + UTP
?
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
-
low activity with AMP
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
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
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
show the reaction diagram
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
show the reaction diagram
the enzme favors ATP as its ligand
-
-
?
dimethylallyl diphosphate + ADP
diphosphate + N6-(dimethylallyl)adenosine 5'-diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine 5'-triphosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0193
ADP
in HEPES (20mM, pH 7.0; 150 mM NaCl, 3 mM dithiothreitol), at 25°C
0.0162
ATP
in HEPES (20mM, pH 7.0; 150 mM NaCl, 3 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
0.759
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
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
0.0195
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
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
0.008
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
0.027
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0109
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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the isopentenyltransferase reaction is the key rate-limiting step in cytokinin biosynthesis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IPT_HUMLU
329
0
36605
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36693
-
x * 36693, calculated from amino acid sequence
37000
-
x * 37000, SDS-PAGE
SUBUNIT
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-NTA resin column chromatography and Mono Q column chromatography
Ni-chelate affinity column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli M15[pREP4] cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakano, Y.; Okada, Y.; Matsunaga, A.; Suwama, T.; Kaneko, T.; Ito, K.; Noguchi, H.; Abe, I.
Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.)
Phytochemistry
65
2439-2446
2004
Humulus lupulus
Manually annotated by BRENDA team
Chu, H.M.; Ko, T.P.; Wang, A.H.
Crystal structure and substrate specificity of plant adenylate isopentenyltransferase from Humulus lupulus: distinctive binding affinity for purine and pyrimidine nucleotides
Nucleic Acids Res.
38
1738-1748
2010
Humulus lupulus (Q5GHF7)
Manually annotated by BRENDA team
Chu, H.M.; Chen, F.Y.; Ko, T.P.; Wang, A.H.
Binding and catalysis of Humulus lupulus adenylate isopentenyltransferase for the synthesis of isopentenylated diadenosine polyphosphates
FEBS Lett.
584
4083-4088
2010
Humulus lupulus
Manually annotated by BRENDA team