2.1.1.341: vanillate/3-O-methylgallate O-demethylase

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For detailed information about vanillate/3-O-methylgallate O-demethylase, go to the full flat file.

Reaction

Synonyms

DesA, LigM, Mtv, syringate O-demethylase, tetrahydrofolate-dependent O-demethylase, vanillate/3-O-methylgallate O-demethylase, vanillate/3MGA O-demethylase

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.341 vanillate/3-O-methylgallate O-demethylase

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Results	in table
1	Activating Compound
3	AA Sequence
4	Cloned(Commentary)
3	Cofactor
2	Crystallization (Commentary)
6	General Information
1	Inhibitors
2	kcat/KM [mM/s]
2	Ki Value [mM]
5	KM Value [mM]
4	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
14	Organism
4	Pathway
4	pH Optimum
2	pH Range
12	Protein Variants
2	Reaction
9	Reference
29	Substrates and Products (Substrate)
5	Subunits
15	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.1.1.341 - vanillate/3-O-methylgallate O-demethylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structure of apo form and in complex with substrates and tetrahydrofolate. Residues His60 and Tyr247 are essential to the catalytic activity of LigM. Their interactions with the oxygen atom in the methoxy group of vanillate seem to facilitate a methyl moiety transfer to tetrahydrofolate

Sphingobium sp.

G2IQS7

740443

to 1.81 A resolution, structure reveals a unique demethylase fold and a canonical folate-binding domain

Sphingomonas paucimobilis

Q60FX1

741347