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Literature summary extracted from

  • Chaiprasongsuk, M.; Zhang, C.; Qian, P.; Chen, X.; Li, G.; Trigiano, R.N.; Guo, H.; Chen, F.
    Biochemical characterization in Norway spruce (Picea abies) of SABATH methyltransferases that methylate phytohormones (2018), Phytochemistry, 149, 146-154 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.141 genes PaSABATH4, PaSABATH5, and PaSABATH10, 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 Picea abies
2.1.1.274 genes PsSABATH2, DNA and amino acid sequence determination and analysis, sequence comparisons, genetic organization and localization of SABATH genes PsSABATH1-10 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 Picea abies
2.1.1.278 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 Picea abies

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.141 Ca2+ inhibition of all isozymes Picea abies
2.1.1.141 Fe2+ inhibition of all isozymes Picea abies
2.1.1.141 Mn2+ inhibition of all isozymes Picea abies
2.1.1.141 Zn2+ strong inhibition of all isozymes Picea abies

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.141 0.0063
-
jasmonate pH 7.0, 18°C, isozyme PtJAMT2 Picea abies
2.1.1.141 0.0146
-
jasmonate pH 7.0, 18°C, isozyme PtJAMT3 Picea abies
2.1.1.141 0.0317
-
jasmonate pH 6.5, 27°C, isozyme PtJAMT1 Picea abies

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.141 additional information K+, Na+, Mg2+, and NH4+ have minimal effect on the isozyme activities Picea abies

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.141 S-adenosyl-L-methionine + jasmonate Picea abies
-
S-adenosyl-L-homocysteine + methyl jasmonate
-
?
2.1.1.274 S-adenosyl-L-methionine + benzoate Picea abies
-
methyl benzoate + S-adenosyl-L-homocysteine
-
?
2.1.1.274 S-adenosyl-L-methionine + salicylate Picea abies
-
methyl salicylate + S-adenosyl-L-homocysteine
-
?
2.1.1.278 S-adenosyl-L-methionine + indole-3-acetic acid Picea abies
-
S-adenosyl-L-homocysteine + methyl indole-3-acetic acid
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.141 Picea abies
-
-
-
2.1.1.274 Picea abies
-
-
-
2.1.1.278 Picea abies
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.141 cone
-
Picea abies
-
2.1.1.141 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 Picea abies
-
2.1.1.141 needle
-
Picea abies
-
2.1.1.274 cone
-
Picea abies
-
2.1.1.274 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 Picea abies
-
2.1.1.274 needle
-
Picea abies
-
2.1.1.278 cone
-
Picea abies
-
2.1.1.278 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 Picea abies
-
2.1.1.278 needle
-
Picea abies
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.141 additional information the isozymes are specific for jasmonate, no or poor activities with indole-3-acetic acid, gibberellic acid 3, or salicylic acid Picea abies ?
-
-
2.1.1.141 S-adenosyl-L-methionine + jasmonate
-
Picea abies S-adenosyl-L-homocysteine + methyl jasmonate
-
?
2.1.1.274 additional information isozyme 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. Radiochemical assay method Picea abies ?
-
-
2.1.1.274 S-adenosyl-L-methionine + benzoate
-
Picea abies methyl benzoate + S-adenosyl-L-homocysteine
-
?
2.1.1.274 S-adenosyl-L-methionine + benzoate 8% activity compared to salicylate Picea abies methyl benzoate + S-adenosyl-L-homocysteine
-
?
2.1.1.274 S-adenosyl-L-methionine + salicylate
-
Picea abies methyl salicylate + S-adenosyl-L-homocysteine
-
?
2.1.1.274 S-adenosyl-L-methionine + salicylate best substrate Picea abies methyl salicylate + S-adenosyl-L-homocysteine
-
?
2.1.1.278 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 Picea abies ?
-
-
2.1.1.278 S-adenosyl-L-methionine + indole-3-acetic acid
-
Picea abies S-adenosyl-L-homocysteine + methyl indole-3-acetic acid
-
?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.141 PaJAMT1
-
Picea abies
2.1.1.141 PaJAMT2
-
Picea abies
2.1.1.141 PaJAMT3
-
Picea abies
2.1.1.141 PaSABATH10
-
Picea abies
2.1.1.141 PaSABATH4
-
Picea abies
2.1.1.141 PaSABATH5
-
Picea abies
2.1.1.274 PaSABATH2
-
Picea abies
2.1.1.274 PaSAMT
-
Picea abies
2.1.1.278 IAA methyltransferase
-
Picea abies
2.1.1.278 PaIAMT
-
Picea abies
2.1.1.278 PaSABATH1
-
Picea abies

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.141 18
-
isozymes PtJAMT2 and PtJAMT3 Picea abies
2.1.1.141 27
-
isozyme PtJAMT1 Picea abies

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.1.141 additional information
-
inactivation of isozyme PtJAMT1 above 40°C, of isozyme PtJAMT2 above 60°C, and of isozyme PtJAMT3 above 50°C Picea abies
2.1.1.141 4 50 activity range of isozymes PtJAMT2 and PtJAMT3, profiles overview Picea abies
2.1.1.141 4 37 activity range of isozyme PtJAMT1, profile overview Picea abies

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.1.141 60
-
activity of all three enzymes is lost when incubated at 60°C for 30 min Picea abies

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.141 6.5
-
isozyme PtJAMT1 Picea abies
2.1.1.141 7
-
isozymes PtJAMT2 and PtJAMT3 Picea abies

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.1.141 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 Picea abies

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.141 S-adenosyl-L-methionine
-
Picea abies
2.1.1.274 S-adenosyl-L-methionine
-
Picea abies
2.1.1.278 S-adenosyl-L-methionine
-
Picea abies

General Information

EC Number General Information Comment Organism
2.1.1.141 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 Picea abies
2.1.1.141 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 Picea abies
2.1.1.274 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 2.1.1.275). 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 Picea abies
2.1.1.274 metabolism indole-3-acetic acid (IAA), gibberellins (GAs), salicylic acid (SA) and jasmonic acid (JA) exist in methyl ester forms in plants in addition to their free acid forms. The enzymes catalyze methylation of these carboxylic acid phytohormones occurs in form of ten isozymes, PaSABATH1-10 Picea abies
2.1.1.278 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 Picea abies
2.1.1.278 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 Picea abies