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Literature summary for 2.1.1.140 extracted from

  • Morris, J.; Yu, L.; Facchini, P.
    A single residue determines substrate preference in benzylisoquinoline alkaloid N-methyltransferases (2020), Phytochemistry, 170, 112193 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E204G mutation to the corresponding residue of Papaver somniferum reticuline N-methyltransferase. Mutant shows a weak activity with (S)-coclaurine and a more substantial activity with (S)-N-methylcoclaurine. Compared to wild-type, activity with (S)-reticuline is 35fold improved Coptis japonica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0102
-
(S)-Coclaurine wild-type, pH 8.0, 30°C Coptis japonica
0.0559
-
(S)-N-methylcoclaurine mutant E204G, pH 8.0, 30°C Coptis japonica
0.072
-
(S)-N-methylcoclaurine wild-type, pH 8.0, 30°C Coptis japonica
0.0799
-
(S)-Coclaurine mutant E204G, pH 8.0, 30°C Coptis japonica

Organism

Organism UniProt Comment Textmining
Coptis japonica Q948P7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + (S)-coclaurine
-
Coptis japonica S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
?
S-adenosyl-L-methionine + (S)-N-methylcoclaurine weak activity Coptis japonica S-adenosyl-L-homocysteine + ?
-
?
S-adenosyl-L-methionine + (S)-reticuline
-
Coptis japonica S-adenosyl-L-homocysteine + (S)-tembetarine
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00031
-
(S)-N-methylcoclaurine wild-type, pH 8.0, 30°C Coptis japonica
0.249
-
(S)-Coclaurine mutant E204G, pH 8.0, 30°C Coptis japonica
0.436
-
(S)-N-methylcoclaurine mutant E204G, pH 8.0, 30°C Coptis japonica
6.28
-
(S)-Coclaurine wild-type, pH 8.0, 30°C Coptis japonica