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Literature summary for 2.1.1.240 extracted from

  • Heo, K.T.; Kang, S.Y.; Hong, Y.S.
    De novo biosynthesis of pterostilbene in an Escherichia coli strain using a new resveratrol O-methyltransferase from Arabidopsis (2017), Microb. Cell Fact., 16, 30 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression in Escherichia coli strains BL21(DE3) and P1, coexpression with genes encoding Saccharothrix espanaensis TAL, Nicotiana tabacum CCL, and Vitis vinifera STS Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information construction of a biological platform to produce pterostilbene with the ROMT gene of Arabidopsis thaliana. Pterostilbene can be synthesized from intracellular L-tyrosine, which requires the activities of four enzymes: tyrosine ammonia lyase (TAL) from Saccharothrix espanaensis, p-coumarate:CoA ligase (CCL) from Nicotiana tabacum, stilbene synthase (STS) from Vitis vinifera, and resveratrol O-methyltransferase (ROMT). For the efficient production of pterostilbene in Escherichia coli, an engineered Escherichia coli strain P1 is used to increase the intracellular pool of L-tyrosine, which is the initial precursor of pterostilbene, with L-mehionine containing media to increase the intracellular pool of S-adenosyl-L-methionine (SAM). Pterostilbene production as high as 33.6 mg/l is achieved, which is about 3.6fold higher compared with that in the parental Escherichia coli strain harboring a plasmid for pterostilbene biosynthesis. Method, overview Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0449
-
trans-resveratrol recombinant enzyme, pH 7.8, 37°C Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + trans-resveratrol Arabidopsis thaliana
-
2 S-adenosyl-L-homocysteine + pterostilbene
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + trans-resveratrol
-
Arabidopsis thaliana 2 S-adenosyl-L-homocysteine + pterostilbene
-
?
additional information mass spectrometric product analysis Arabidopsis thaliana ?
-
-

Synonyms

Synonyms Comment Organism
resveratrol O-methyltransferase
-
Arabidopsis thaliana
ROMT
-
Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Arabidopsis thaliana

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0128
-
trans-resveratrol recombinant enzyme, pH 7.8, 37°C Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function the multifunctional caffeic acid O-methyltransferase (COMT, EC 2.1.1.46) originating from Arabidopsis thaliana also catalyzes the transfer of a methyl group to resveratrol resulting in pterostilbene production (EC 2.1.1.240) Arabidopsis thaliana

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.285
-
trans-resveratrol recombinant enzyme, pH 7.8, 37°C Arabidopsis thaliana