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Information on EC 2.1.1.278 - indole-3-acetate O-methyltransferase
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EC Tree
2.1.1.278 indole-3-acetate O-methyltransferaseIUBMB Comments
Binds Mg2+. The enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone .
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Word Map
- 2.1.1.278
- auxin
-
phytohormone
-
hypocotyls
- shoot
- methyltransferases
- lamina
-
sabaths
- flower
-
auxin-responsive
- poplar
- esterase
-
mimicry
-
hyponastic
-
curling
-
curvature
-
dr5-gus
-
rosette
-
semi-dwarfism
-
meristem
- biotechnology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
iamt1, ptiamt1, iaa carboxyl methyltransferase, atiamt1, osiamt1, ossabath4, pasabath1, iaa methyltransferase, iaa methyltransferase1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IAA methyltransferase
IAMT
IAMT1
indole-3-acetic acid methyltransferase
S-adenosyl-L-methionine:salicylic acid carboxyl methyltransferase
UniProt
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + (indol-3-yl)acetate = S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:(indol-3-yl)acetate O-methyltransferase
Binds Mg2+. The enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone [2].
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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
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
S-adenosyl-L-methionine + (indol-3-yl)butyrate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)butyrate
S-adenosyl-L-methionine + dichlorophenoxyacetic acid
S-adenosyl-L-homocysteine + ?
at 5% of the catalytic activity compared to (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + farnesoate
methyl farnesoate + S-adenosyl-L-homocysteine
low activity
-
-
?
S-adenosyl-L-methionine + indole-3-acetate
methyl indole-3-acetate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + indole-3-acetic acid
S-adenosyl-L-homocysteine + methyl indole-3-acetic acid
-
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
the enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
the enzyme modulates homeostasis of (indol-3-yl)acetate in plant tissues through methylation of the free carboxyl group of (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
the enzyme modulates homeostasis of (indol-3-yl)acetate in plant tissues through methylation of the free carboxyl group of (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
highest activity
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)butyrate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)butyrate
at 2% of the catalytic activity compared to (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)butyrate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)butyrate
-
11% activity compared to (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + indole-3-acetate
methyl indole-3-acetate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + indole-3-acetate
methyl indole-3-acetate + S-adenosyl-L-homocysteine
-
-
-
?
additional information
?
-
no activity with: salicylate, jasmonic acid, farnesoic acid and gibberellic acid
-
-
?
additional information
?
-
-
PaSABATH1 has the highest level of specific activity with IAA and is renamed as PaIAMT. No activity with salicylic acid, jasmonic acid, and giberellic acid 3
-
-
-
additional information
?
-
-
no activity with salicylic acid, benzoic acid, jasmonic acid, and farnesoic acid
-
-
?
additional information
?
-
PtSABATH1, also named PtIAMT1, can catalyze the formation of methyl indole-3-acetate (MeIAA) using SAM as a methyl donor and indole-3-acetic acid (IAA) as a methyl acceptor. Enzyme PtSABATH1 does not show any activity towards substrates benzoic acid, jasmonic acid, salicylic acid, vanillic acid, nicotinic acid, coumalic acid, or trans-cinnamic acid. Compared with other Populus SABATH proteins (PtSABATH2, 3, 12, 17, 21 and 24 have very weak activities towards IAA), PtSABATH1 shows at least 40.5fold higher activity towards IAA
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-
-
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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
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
S-adenosyl-L-methionine + indole-3-acetate
methyl indole-3-acetate + S-adenosyl-L-homocysteine
S-adenosyl-L-methionine + indole-3-acetic acid
S-adenosyl-L-homocysteine + methyl indole-3-acetic acid
-
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
the enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
the enzyme modulates homeostasis of (indol-3-yl)acetate in plant tissues through methylation of the free carboxyl group of (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
the enzyme modulates homeostasis of (indol-3-yl)acetate in plant tissues through methylation of the free carboxyl group of (indol-3-yl)acetate
-
-
?
S-adenosyl-L-methionine + (indol-3-yl)acetate
S-adenosyl-L-homocysteine + methyl (indol-3-yl)acetate
-
highest activity
-
-
?
S-adenosyl-L-methionine + indole-3-acetate
methyl indole-3-acetate + S-adenosyl-L-homocysteine
-
-
-
?
S-adenosyl-L-methionine + indole-3-acetate
methyl indole-3-acetate + S-adenosyl-L-homocysteine
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Na+
NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infertility, Male
Reduction of indole-3-acetic acid methyltransferase activity compensates for high-temperature male sterility in Arabidopsis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66.51
recombinant wild-type PtSABATH1 with indole-3-acetate, pH 7.4, 25°C
8.98
recombinant wild-type PtSABATH4 with farnesoic acid, pH 7.4, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
pH 6.5: 20% of maximal activity, pH 9.0: 30% of maximal activity
6.7 - 9
-
at pH 6.5, the enzyme has about 34% of its maximal activity, whereas at pH 9.0, the enzyme displays about 40% of the maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression profile of IAMT1 in flower tissues, overview
brenda
additional information
-
moderate expression in young leaves, no expression in old leaves
brenda
additional information
the IAMT1 gene is widely expressed in all Arabidopsis thaliana organs
brenda
additional information
-
the IAMT1 gene is widely expressed in all Arabidopsis thaliana organs
brenda
additional information
-
mixed tissues including needles, stems, and young male cones and female cones are collected from a mature Norway spruce (Picea abies) tree grown on the campus of the University of Tennessee, Knoxville, TN with a GPS coordinates of 35.948 and -83.942
brenda
additional information
gene PtSABATH1 is expressed in the root, shoot, leaf and bud tissues, but not expressed in the Populus flower
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
overexpression of IAMT1 causes a decrease in auxin signalling. Reduction of indole-3-acetic acid methyltransferase activity compensates for high-temperature male sterility in Arabidopsis thaliana. Attenuation of IAMT1 activity promotes fertilization and enhances thermotolerance. The iamt1 mutant shows increased auxin signalling in funiculi, which correlated with a higher growth rate of wild-type pollen in contact with mutant ovaries and premature ovule fertilization. While the production of seeds per fruit is similar in the wild-type and the mutant at 20°C, exposure to 29°C causes a more severe decrease in fertility in the wild-type than in the mutant. Loss of IAMT1 activity is also associated with the production of more nodes after flowering and higher tolerance of the shoot apical meristem to higher temperatures. As a consequence, the productivity of the iamt1 mutant under higher temperatures is more than double of that of the wild-type, with almost no apparent trade-off
metabolism
expression patterns of Populus SABATH genes under normal growth conditions and abiotic stress, overview
physiological function
additional information
-
a structural model for PaIAMTis generated to understand the origin of substrate specificity of PaSABATH methyltransferase. The active site of the PaIAMT model is superposed with that of the X-ray structure of IAMT (PDB ID 3B5I). The substrate indole-3-acetic acid (IAA) is docked into the active site in such way that its carboxyl moiety is located at a suitable position for accepting the methyl group from SAM (AdoMet). The active site of the enzymes is able to accommodate IAA in a reactive configuration. The enzyme has relatively high specificity for IAA. This is in contrast to docking jasmonate (JA) into the active site. When JA is docked into the active sites with the carboxyl moiety located at the suitable position for accepting the methyl group, the side chain of JA made steric clashes with some of the active site residues (F267 and L266 from PaIAMT), and the active site is therefore not able to accommodate JA for the methyl transfer
evolution
-
the enzyme belongs to the protein family of SABATH methyltransferases, ten genes encode isozymes PaSABATH1-10. Five of the PaSABATH isozymes (PaSABATH3, PaSABATH6, PaSABATH7, PaSABATH8, and PaSABATH9) do not show activity with any of the four substrates, i.e. indole-3-acetic acid, jasmonic acid, giberellic acid A3, and salicylic acid, the other five of the PaSABATHs each show activity with one or more of the four substrates. PaSABATH1 has the highest level of specific activity with indole-3-acetic acid and is renamed as PaIAMT (EC 2.1.1.278). PaSABATH2 has the highest level of specific activity with salicylic acid and is designated as PaSAMT (EC 2.1.1.274). For comparison, PaSAMT is also assayed with two compounds of similar structure benzoic acid and anthranilic acid (cf. EC 2.1.1.273). While PaSAMT has no activity with anthranilic acid, its activity with benzoic acid is approximately 8% of that with salicylic acid. PaSABATH4, PaSABATH5 and PaSABATH10 show the highest level of specific activity with jasmonic acid and are renamed PaJAMT1, PaJAMT2, and PaJAMT3, respectively (EC 2.1.1.141). Their products are confirmed to be methyljasmonate
evolution
the enzyme belongs to the SABATH family, phylogenetic analysis and tree, detailed overview. Twenty-eight Populus SABATH genes are divided into three classes with distinct divergences in their gene structure, expression responses to abiotic stressors and enzymatic properties of encoded proteins. Populus class I SABATH proteins convert indole-3-acetic acid (IAA) to methyl-IAA, class II SABATH proteins convert benzoic acid (BA) and salicylic acid (SA) to methyl-BA and methyl-SA, while class III SABATH proteins convert farnesoic acid (FA) to methyl-FA. Populus class I SABATH gene (PtSABATH1) is grouped into clade I, Populus contains only one class I SABATH gene (PtSABATH1)
physiological function
the enzyme is found in plants and is important for regulation of the plant hormone (indol-3-yl)acetate. The product, methyl (indol-3-yl)acetate is inactive as hormone
physiological function
-
the enzyme is involved in development of root and leaf in poplar and plays a role in wood formation
physiological function
the enzyme regulated leaf development. Overexpression of isoform IAMT1 in abaxial layers results in epinastic leaf phenotypes
physiological function
of Populus SABATH enzymes, only PtSABATH1 has high activity towards indole-3-acetic acid (IAA), and can convert IAA to methyl-IAA, indicating that PtSABATH1 might play an important role in auxin homeostasis
physiological function
plant hormone auxin induces temperature tolerance to pollen. Methylation of indole-3-acetic acid (IAA) by indole-3-acetic acid methyltransferase has been shown to participate in auxin homeostasis. Methyl-IAA (Me-IAA) is an inactive form of IAA
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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). IAMT1_ARATH
386
0
42054
Swiss-Prot
other Location (Reliability: 3)
IAMT1_ORYSJ
404
0
43751
Swiss-Prot
other Location (Reliability: 5)
G7K8Q3_MEDTR
392
0
42770
TrEMBL
other Location (Reliability: 2)
A0A2G9I0P5_9LAMI
383
0
42076
TrEMBL
other Location (Reliability: 3)
A0A396IP87_MEDTR
194
0
21238
TrEMBL
other Location (Reliability: 2)
A0A396INA2_MEDTR
211
0
23265
TrEMBL
other Location (Reliability: 2)
A0A072UXX4_MEDTR
382
0
41955
TrEMBL
other Location (Reliability: 2)
A0A5B7BUS0_DAVIN
162
0
17752
TrEMBL
other Location (Reliability: 3)
A0A5B7BNJ3_DAVIN
189
0
21396
TrEMBL
other Location (Reliability: 2)
A0A2P6QCU6_ROSCH
386
0
42311
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the enzyme is determined and refined to 2.75 A resolution
the crystal structure of the enzyme is determined and refined to 2.75 A resolution
the crystal structure of the enzyme is determined and refined to 2.75 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
targeted nuclear expression of Triticum aestivum gene TaWRKY71-1, encoding a WRKY transcription factor, in Arabidopsis thaliana induces the expression if gene IAMT1. TaWRKY71-1 localizes in the nucleus and has no transcriptional activation activity. TaWRKY71-1 overexpression in Arabidopsis results in hyponastic rosette leaves, and the hyponastic strength is closely correlative with the transcription level of the transgene. The spongy mesophyll cells at abaxial side of leaves are drastically compacted by TaWRKY71-1 overexpression
additional information
-
targeted nuclear expression of Triticum aestivum gene TaWRKY71-1, encoding a WRKY transcription factor, in Arabidopsis thaliana induces the expression if gene IAMT1. TaWRKY71-1 localizes in the nucleus and has no transcriptional activation activity. TaWRKY71-1 overexpression in Arabidopsis results in hyponastic rosette leaves, and the hyponastic strength is closely correlative with the transcription level of the transgene. The spongy mesophyll cells at abaxial side of leaves are drastically compacted by TaWRKY71-1 overexpression
additional information
construction of the T-DNA insertion mutant iamt1-1. Increasing indole-3-acetic acid (IAA) in ovaries by reducing IAA methyltransferase1 (IAMT1) activity in Arabidopsis thaliana, phenotype, overview. Loss of IAMT1 activity is also associated with the production of more nodes after flowering and higher tolerance of the shoot apical meristem to higher temperatures. As a consequence, the productivity of the iamt1 mutant under higher temperatures is more than double of that of the wild-type, with almost no apparent trade-off
additional information
-
construction of the T-DNA insertion mutant iamt1-1. Increasing indole-3-acetic acid (IAA) in ovaries by reducing IAA methyltransferase1 (IAMT1) activity in Arabidopsis thaliana, phenotype, overview. Loss of IAMT1 activity is also associated with the production of more nodes after flowering and higher tolerance of the shoot apical meristem to higher temperatures. As a consequence, the productivity of the iamt1 mutant under higher temperatures is more than double of that of the wild-type, with almost no apparent trade-off
additional information
-
targeted nuclear expression of Triticum aestivum gene TaWRKY71-1, encoding a WRKY transcription factor, in Arabidopsis thaliana induces the expression if gene IAMT1. TaWRKY71-1 localizes in the nucleus and has no transcriptional activation activity. TaWRKY71-1 overexpression in Arabidopsis results in hyponastic rosette leaves, and the hyponastic strength is closely correlative with the transcription level of the transgene. The spongy mesophyll cells at abaxial side of leaves are drastically compacted by TaWRKY71-1 overexpression
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene PaSABATH1, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization and localization of SABATH genes in the genome of Picea abies, overview. Sequence similarities among PaSABATHs range from 49% to 91%. Most PaSABATH genes have three introns with the exception of PaSABATH4, PaSABATH5 and PaSABATH10, each of which contains two introns. Phylogenetic analysis and tree
-
gene SABATH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overview, recombinant expression of soluble His-tagged enzyme in Escherichia coli strain BL21(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
targeted nuclear expression of Triticum aestivum gene TaWRKY71-1, encoding a WRKY transcription factor, in Arabidopsis thaliana induces the expression if gene IAMT1
targeted nuclear expression of Triticum aestivum gene TaWRKY71-1, encoding a WRKY transcription factor, in Arabidopsis thaliana induces the expression if gene IAMT1
targeted nuclear expression of Triticum aestivum gene TaWRKY71-1, encoding a WRKY transcription factor, in Arabidopsis thaliana induces the expression if gene IAMT1
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
potential use of reducing IAA methyltransferase activity as a method to enhance reproductive success in plants
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, L.; Hou, X.; Tsuge, T.; Ding, M.; Aoyama, T.; Oka, A.; Gu, H.; Zhao, Y.; Qu, L.J.
The possible action mechanisms of indole-3-acetic acid methyl ester in Arabidopsis
Plant Cell Rep.
27
575-584
2008
Arabidopsis thaliana (Q9FLN8)
brenda