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Literature summary for 2.1.1.140 extracted from

  • Liscombe, D.K.; Facchini, P.J.
    Molecular cloning and characterization of tetrahydroprotoberberine cis-N-methyltransferase, an enzyme involved in alkaloid biosynthesis in opium poppy (2007), J. Biol. Chem., 282, 14741-14751.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Papaver somniferum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + (S)-coclaurine Papaver somniferum
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S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
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?

Organism

Organism UniProt Comment Textmining
Papaver somniferum Q7XB08 cv. Marianne, opium poppy
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Source Tissue

Source Tissue Comment Organism Textmining
root sequence comparison Papaver somniferum
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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phylogenetic analysis reveales a monophyletic clade for (S)-coclaurine N-methyltransferase (CNMT) and (S)-tetrahydroprotoberberine cis-N-methyltransferase (TNMT), 48% identity of amino acid sequence, downstream metabolic role suggests that TNMT derives from gene duplication after more ancient recruitment of CNMT, phylogenetic relationship between CNMT and TNMT provides new insights into evolutionary recruitment of enzymes into plant alkaloid pathways Papaver somniferum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + (S)-coclaurine
-
Papaver somniferum S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
?
S-adenosyl-L-methionine + (S)-coclaurine analysis of the evolutionary recruitment of enzymes into plant alkaloid pathways Papaver somniferum S-adenosyl-L-homocysteine + (S)-N-methylcoclaurine
-
?

Synonyms

Synonyms Comment Organism
(S)-Coclaurine N-methyltransferase
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Papaver somniferum
CNMT
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Papaver somniferum