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Information on EC 2.1.1.141 - jasmonate O-methyltransferase
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EC Tree
2.1.1.141 jasmonate O-methyltransferaseIUBMB Comments
9,10-Dihydrojasmonic acid is a poor substrate for the enzyme. The enzyme does not convert 12-oxo-phytodienoic acid (a precursor of jasmonic acid), salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters. Enzyme activity is inhibited by the presence of divalent cations, e.g., Ca2+, Cu2+, Mg2+ and Zn2+.
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Word Map
- 2.1.1.141
-
l-isoaspartyl
-
d-aspartyl
-
methyl-accepting
-
technologists
-
s-adenosyl-l-methyl-3hmethionine
-
2.1.1.77
-
prenylcysteine
-
sabaths
-
3h-methylated
-
age-damaged
- agriculture
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
carboxyl methyltransferase, jamt, jasmonic acid carboxyl methyltransferase, atjmt, ja carboxyl methyltransferase, s-adenosyl-l-methionine:jasmonic acid carboxyl methyltransferase, jasmonate o-methyltransferase, pasabath4, pasabath5, pasabath10, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
jasmonic acid carboxyl methyltransferase
JMT
JMT1
S-adenosyl-L-methionine:jasmonic acid carboxyl methyltransferase
jasmonic acid carboxyl methyltransferase
-
-
-
-
JMT
-
-
-
-
S-adenosyl-L-methionine:jasmonic acid carboxyl methyltransferase
-
-
-
-
S-adenosyl-L-methionine:jasmonic acid carboxyl methyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:jasmonate O-methyltransferase
9,10-Dihydrojasmonic acid is a poor substrate for the enzyme. The enzyme does not convert 12-oxo-phytodienoic acid (a precursor of jasmonic acid), salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters. Enzyme activity is inhibited by the presence of divalent cations, e.g., Ca2+, Cu2+, Mg2+ and Zn2+.
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CAS REGISTRY NUMBER
COMMENTARY
346420-58-4
-
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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 + 9,10-dihydrojasmonic acid
S-adenosyl-L-homocysteine + ?
poor substrate
-
-
?
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
22% activity compared to jasmonate
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
expression of the gene is induced both locally and systematically by wounding or methyl jasmonate treatement. The jasmonic acid carboxyl methyltransferase is a key enzyme for jasmonate-regulated plant responses. Activation of JMT expression leads to production of methyl jasmonate that could act as an intracellular regulator, a diffusible intercellular transducer, and an airborne signal mediating intra- and interplant communications
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
methyl jasmonate modulates diverse developmental processes and defense responses in plants, acting as an important cellular regulator
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
methyljasmonate formation is a key control point for jasmonate-responsive gene expression in plants, overview
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
additional information
?
-
the enzyme does not convert 12-oxo-phytodienoic acid, a precursor of jasmonic acid, salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters
-
-
?
additional information
?
-
-
the enzyme does not convert 12-oxo-phytodienoic acid, a precursor of jasmonic acid, salicylic acid, benzoic acid, linolenic acid or cinnamic acid into their corresponding methyl esters
-
-
?
additional information
?
-
-
the enzyme activity with benzoate and salicylate as substrates is less than 1.5% of that with jasmonate
-
-
?
additional information
?
-
-
the enzyme activity with benzoate and salicylate as substrates is less than 1.5% of that with jasmonate
-
-
?
additional information
?
-
-
the isozymes are specific for jasmonate, no or poor activities with indole-3-acetic acid, gibberellic acid 3, or salicylic acid
-
-
-
additional information
?
-
no activity with salicylic acid, indole-3-acetic acid, and gibberellic acid
-
-
?
additional information
?
-
-
no activity with salicylic acid, indole-3-acetic acid, and gibberellic acid
-
-
?
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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 + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
expression of the gene is induced both locally and systematically by wounding or methyl jasmonate treatement. The jasmonic acid carboxyl methyltransferase is a key enzyme for jasmonate-regulated plant responses. Activation of JMT expression leads to production of methyl jasmonate that could act as an intracellular regulator, a diffusible intercellular transducer, and an airborne signal mediating intra- and interplant communications
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
methyl jasmonate modulates diverse developmental processes and defense responses in plants, acting as an important cellular regulator
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
methyljasmonate formation is a key control point for jasmonate-responsive gene expression in plants, overview
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
?
S-adenosyl-L-methionine + jasmonate
S-adenosyl-L-homocysteine + methyl jasmonate
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
additional information
-
K+, Na+, Mg2+, and NH4+ have minimal effect on the isozyme activities
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
5 mM Ca2+ shows a mild inhibition effect on enzyme activity (about 80% residual activity)
Mg2+
shows a mild inhibition effect on enzyme activity (about 85% residual activity)
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
High levels of protein carboxyl methyltransferase in well-differentiated human endometrial carcinoma.
Endometrial Neoplasms
High levels of protein carboxyl methyltransferase in well-differentiated human endometrial carcinoma.
Leukemia
Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells.
Neuroblastoma
Methylation of 21-23 kD membrane proteins by a membrane-associated protein carboxyl methyltransferase in neuroblastoma cells. Increased methylation in differentiated cells.
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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.11
0.18
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
inactivation of isozyme PtJAMT1 above pH 8.0, of isozyme PtJAMT2 above pH 8.5, and of isozyme PtJAMT3 above pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
inactivation of isozyme PtJAMT1 above 40°C, of isozyme PtJAMT2 above 60°C, and of isozyme PtJAMT3 above 50°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
expression is gradually down-regulated with the development of seeds
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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
overexpression of enzyme in the Glycine max seeds results in decreased amounts of tryptophan, palmitic acid, linolenic acid, and stachyose, but increased levels of gadoleic acid and genistein. In particular, seeds contain 120.0-130.5% more genistein and 60.5-82.1% less stachyose than the wild type
physiological function
additional information
-
structural modeling of isozymes PaJAMT1 and PaJAMT3, docking structures with Indole-3-acetic acid (IAA) suggest that the active-site residues (e.g. V339 and F343 from PaJAMT1 and M347 and F351 from PaJAMT3) interfere with IAA binding for the methyl transfer, and this is consistent with the relatively low activities of these two enzymes toward IAA.When jasmonate (JA) is docked into the active sites of PaJAMT1 and PaJAMT3, the steric clashes with the active site residues are not observed, and this observation structurally validates that they are jasmonate methyltransferases, JAMTs
physiological function
the enzyme plays a role in plant defense against biotic stresses
physiological function
the enzyme plays a role in regulating plant development as well as herbivore-induced defense responses in rice
physiological function
-
ectopic expression of JMT in tomato does not increase the methyl jasmonate content, while the expression levels of endogenous methyl jasmonate biosynthesis genes are influenced, especially in the wound treatment
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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). JMT_BRARP
392
0
43816
Swiss-Prot
other Location (Reliability: 2)
JMT1_THECC
373
0
41465
Swiss-Prot
other Location (Reliability: 3)
JMT2_THECC
373
0
41388
Swiss-Prot
other Location (Reliability: 2)
JMT_ARATH
389
0
43443
Swiss-Prot
other Location (Reliability: 3)
A0A5B7BIE8_DAVIN
170
0
19000
TrEMBL
other Location (Reliability: 3)
A0A0B2RN67_GLYSO
327
0
36917
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7C8YUH2_OPUST
248
0
28107
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7C8Z0M1_OPUST
117
0
12985
TrEMBL
other Location (Reliability: 3)
B9T2Q9_RICCO
330
0
37143
TrEMBL
other Location (Reliability: 3)
A0A2G9I2T0_9LAMI
175
0
19437
TrEMBL
other Location (Reliability: 3)
A0A7C9ER34_OPUST
399
0
45148
TrEMBL
Mitochondrion (Reliability: 4)
B9T7V8_RICCO
375
0
42315
TrEMBL
other Location (Reliability: 2)
A0A088Q2I5_ARTAN
366
0
40785
TrEMBL
other Location (Reliability: 2)
A0A5B6YH75_DAVIN
371
0
41905
TrEMBL
other Location (Reliability: 2)
A0A2P6PYT8_ROSCH
150
0
17056
TrEMBL
other Location (Reliability: 3)
A0A0B2Q6J3_GLYSO
346
0
39589
TrEMBL
other Location (Reliability: 3)
B9S6C3_RICCO
366
0
40958
TrEMBL
other Location (Reliability: 2)
A0A2I0AXP3_9ASPA
405
0
46314
TrEMBL
other Location (Reliability: 5)
A0A7C9EMJ4_OPUST
342
0
38425
TrEMBL
other Location (Reliability: 3)
A0A7C8YU87_OPUST
110
0
12174
TrEMBL
other Location (Reliability: 3)
A0A2I0A4M8_9ASPA
105
0
11935
TrEMBL
other Location (Reliability: 3)
A0A7C9A3Z8_OPUST
243
0
27452
TrEMBL
other Location (Reliability: 3)
A0A7C9CUC7_OPUST
229
0
25648
TrEMBL
other Location (Reliability: 3)
B9S6C1_RICCO
366
0
40748
TrEMBL
other Location (Reliability: 2)
A0A2P6R3D0_ROSCH
406
0
45602
TrEMBL
other Location (Reliability: 4)
A0A0B2QMV6_GLYSO
370
0
41592
TrEMBL
other Location (Reliability: 4)
A0A2I0AXR3_9ASPA
191
0
22044
TrEMBL
other Location (Reliability: 4)
A0A7C8ZN32_OPUST
145
0
16635
TrEMBL
other Location (Reliability: 3)
B9SYY5_RICCO
386
0
42525
TrEMBL
other Location (Reliability: 5)
A0A396JLG5_MEDTR
148
0
17084
TrEMBL
other Location (Reliability: 2)
A0A7C9A303_OPUST
109
0
12254
TrEMBL
other Location (Reliability: 3)
A0A7C9A3H5_OPUST
132
0
15018
TrEMBL
other Location (Reliability: 2)
A0A7C8YT27_OPUST
110
0
12298
TrEMBL
other Location (Reliability: 3)
I0DHG9_CYMEN
374
0
42024
TrEMBL
other Location (Reliability: 3)
A0A7C9A4J6_OPUST
178
0
19965
TrEMBL
other Location (Reliability: 3)
A0A7C9ECR0_OPUST
344
0
39087
TrEMBL
Mitochondrion (Reliability: 5)
A0A7C8YMU2_OPUST
233
0
26590
TrEMBL
Mitochondrion (Reliability: 5)