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Information on EC 2.5.1.27 - adenylate dimethylallyltransferase and Organism(s) Humulus lupulus and UniProt Accession Q5GHF7
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2.5.1.27 adenylate dimethylallyltransferaseIUBMB Comments
Involved in the biosynthesis of cytokinins in plants. Some isoforms from the plant Arabidopsis thaliana are specific for AMP while others also have the activity of EC 2.5.1.112, adenylate dimethylallyltransferase (ADP/ATP-dependent).
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Word Map
- 2.5.1.27
- tumefaciens
- trans-zeatin
-
marker-free
- zeatin
- isopentenyladenine
-
tz-type
-
bentgrass
- stolonifera
-
senescence-activated
- cis-zeatin
-
agrostis
- synthesis
The taxonomic range for the selected organisms is: Humulus lupulus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
isopentenyl transferase, isopentenyltransferase, sag12-ipt, atipt3, atipt5, adenosine phosphate-isopentenyltransferase, ipt5b, atipt7, adenylate isopentenyltransferase, atipt4, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HlAIPT
adenylate isopentenyltransferase-ATP complex from Humulus lupulus
2-isopentenyl-diphosphate:AMP DELTA2-isopentenyltransferase
-
-
-
-
cytokinin synthase
-
-
-
-
dimethylallyl-diphosphate:AMP DELTA2-isopentenyltransferase
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-
-
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dimethylallylpyrophosphate:5'-AMP transferase
-
-
-
-
DMA transferase
-
-
-
-
isopentenyltransferase
-
-
-
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isopentenyltransferase, adenylate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkenyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:AMP dimethylallyltransferase
Involved in the biosynthesis of cytokinins in plants. Some isoforms from the plant Arabidopsis thaliana are specific for AMP while others also have the activity of EC 2.5.1.112, adenylate dimethylallyltransferase (ADP/ATP-dependent).
CAS REGISTRY NUMBER
COMMENTARY
72840-95-0
-
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
dimethylallyl diphosphate + ADP
?
the enzyme prefers ADP and ATP rather than AMP
-
-
?
dimethylallyl diphosphate + AMP
diphosphate + N-(dimethylallyl)adenosine 5'-phosphate
-
-
-
ir
dimethylallyl diphosphate + AMP
diphosphate + N6-(dimethylallyl)adenosine 5'-phosphate
the enzyme prefers ADP and ATP rather than AMP
-
-
?
dimethylallyl diphosphate + ATP
?
the enzyme prefers ADP and ATP rather than AMP
-
-
?
dimethylallyl diphosphate + ATP
N6-(dimethylallyl) adenosine 5'-triphosphate + diphosphate
-
-
-
ir
dimethylallyl diphosphate + ATP
diphosphate + N6-(dimethylallyl)adenosine triphosphate
-
-
-
-
?
additional information
?
-
no activity with GMP, IMP, CMP and UMP
-
-
?
additional information
?
-
-
the plant AIPT predominantly uses ATP or ADP as the isopentenyl acceptor
-
-
?
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
dimethylallyl diphosphate + AMP
diphosphate + N-(dimethylallyl)adenosine 5'-phosphate
-
-
-
ir
dimethylallyl diphosphate + ATP
N6-(dimethylallyl) adenosine 5'-triphosphate + diphosphate
-
-
-
ir
additional information
?
-
-
the plant AIPT predominantly uses ATP or ADP as the isopentenyl acceptor
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
initial reaction in the biosynthesis of cytokinins, which are important plant hormones
metabolism
-
cytokinins are important adenine-base phytohormones which promote cell division and their biosynthesis has two pathways depending on different substrates. The first pathway begins with the transfer of isopentenyl group from dimethylallyl diphosphate to the N6-amino group of AMP, ADP or ATP by adenylate isopentenyltransferase, AIPT
physiological function
-
the isopentenyltransferase reaction is the key rate-limiting step in cytokinin biosynthesis that transfers the isopentenyl group from dimethylallyl diphosphate to the N6-amino group of adenine
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). IPT_HUMLU
329
0
36605
Swiss-Prot
Chloroplast (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
The crystal structure of the AIPT-ATP complex from Humulus lupulus is similar to the previous structures of Agrobacterium AIPT and yeast tRNA-IPT. The enzyme is structurally homologous to the NTP-binding kinase family of proteins but forms a solvent-accessible channel that binds to the donor substrate dimethylallyl diphosphate, which is directed toward the acceptor substrate ATP/ADP.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpressed as a N-terminal hexahistidine tag protein in Escherichia coli BL21 (DE3)
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 (Q5GHF7), Humulus lupulus
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), Humulus lupulus
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