Entry Name 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol 3-C-methyltransferase;
Class Transferases;BRITE hierarchy
Sysname S-adenosyl-L-methionine:6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol 3-C-methyltransferase
Reaction(IUBMB) S-adenosyl-L-methionine + 6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol = S-adenosyl-L-homocysteine + 6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol [RN:
R13499 ]
Reaction(KEGG) Substrate S-adenosyl-L-methionine [CPD:
C00019 ];
6-carboxymethyl-5-methyl-4-hydroxypyridin-2-ol [CPD:
C23037 ]
Product S-adenosyl-L-homocysteine [CPD:
C00021 ];
6-carboxymethyl-3,5-dimethyl-4-hydroxypyridin-2-ol [CPD:
C23038 ]
Comment The enzyme, characterized from the archaeon Methanococcus maripaludis, participates in the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor of EC
1.12.98.2 , 5,10-methenyltetrahydromethanopterin hydrogenase (also known as [Fe]-hydrogenase).
History EC 2.1.1.400 created 2025
Reference Authors Fujishiro T, Bai L, Xu T, Xie X, Schick M, Kahnt J, Rother M, Hu X, Ermler U, Shima S.
Title Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.
Journal Sequence Reference Authors Bai L, Fujishiro T, Huang G, Koch J, Takabayashi A, Yokono M, Tanaka A, Xu T, Hu X, Ermler U, Shima S.
Title Towards artificial methanogenesis: biosynthesis of the [Fe]-hydrogenase cofactor and characterization of the semi-synthetic hydrogenase.
Journal Reference Authors Schaupp S, Arriaza-Gallardo FJ, Pan HJ, Kahnt J, Angelidou G, Paczia N, Costa K, Hu X, Shima S.
Title In Vitro Biosynthesis of the [Fe]-Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors.
Journal Sequence Other DBs ExPASy - ENZYME nomenclature database: 2.1.1.400
LinkDB All DBs
