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Literature summary for 2.1.1.232 extracted from

  • Murata, K.; Kitano, T.; Yoshimoto, R.; Takata, R.; Ube, N.; Ueno, K.; Ueno, M.; Yabuta, Y.; Teraishi, M.; Holland, C.; Jander, G.; Okumoto, Y.; Mori, N.; Ishihara, A.
    Natural variation in the expression and catalytic activity of a naringenin 7-O-methyltransferase influences antifungal defenses in diverse rice cultivars (2019), Plant J., 101, 1103-1117 .
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Oryza sativa

Protein Variants

Protein Variants Comment Organism
additional information domain swapping experiments between Nipponbare and Kasalath NOMT genes. The replacement of the Kasalath O-methyltransferase domain with the Nipponbare domain increases the enzyme activity to the level of the Nipponbare enzyme Oryza sativa
T130P mutation in cultivar Kassalth gene to match the corresonding residue in cultivar Nipponbare. Mutant shows activity comparable to Nipponbare NOMT Oryza sativa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.15
-
 (2S)-naringenin cultivar Kassalath, pH 9.5, 30°C Oryza sativa
1.38
-
 (2S)-naringenin cultivar Nipponbare, pH 9.5, 30°c Oryza sativa
4.27
-
 S-adenosyl-L-methionine cultivar Nipponbare, pH 9.5, 30°c Oryza sativa
19.3
-
 S-adenosyl-L-methionine cultivar Kassalath, pH 9.5, 30°C Oryza sativa

Organism

Organism UniProt Comment Textmining
Oryza sativa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Oryza sativa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + (2S)-naringenin
-
 Oryza sativa S-adenosyl-L-homocysteine + (2S)-sakuranetin
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.03
-
 S-adenosyl-L-methionine cultivar Kassalath, pH 9.5, 30°C Oryza sativa
26
-
 S-adenosyl-L-methionine cultivar Nipponbare, pH 9.5, 30°C Oryza sativa

General Information

General Information Comment Organism
physiological function leaves of rice cultivar Nipponbare predominantly accumulate the phytoalexin sakuranetin after jasmonic acid induction. The Kasalath cultivar accumulates only low amounts of sakuranetin. Both NOMT expression and NOMT enzymatic activity are lower in Kasalath than in Nipponbare. A proline to threonine substitution in Kasalath relative to Nipponbare NOMT is the main cause of the lower enzymatic activity. The relative amounts of naringenin and sakuranetin may provide protection against specific pathogen profiles in different rice-growing environments. Naringenin is more effective against bacterial pathogens and sakuranetin is more effective against fungal pathogens Oryza sativa