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Literature summary for 2.1.1.141 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
Search for more literature for 2.1.1.141

Cloned(Commentary)

Cloned (Comment) Organism
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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + jasmonate Picea abies
-
 S-adenosyl-L-homocysteine + methyl jasmonate
-
 ?

Organism

Organism UniProt Comment Textmining
Picea abies
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cone
-
 Picea abies
-
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
-
needle
-
 Picea abies
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
-
S-adenosyl-L-methionine + jasmonate
-
 Picea abies S-adenosyl-L-homocysteine + methyl jasmonate
-
 ?

Synonyms

Synonyms Comment Organism
PaJAMT1
-
 Picea abies
PaJAMT2
-
 Picea abies
PaJAMT3
-
 Picea abies
PaSABATH10
-
 Picea abies
PaSABATH4
-
 Picea abies
PaSABATH5
-
 Picea abies

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Picea abies

General Information

General Information Comment Organism
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
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