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IUBMB Comments Requires Mg2+ Mycolicibacterium hassiacum , participates in the biosynthesis of 3-O -methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in nontuberculous mycobacteria. The methylation catalysed by this enzyme was shown to block the reducing end of 3,3′-di-O -methyl-α-mannobiose, a probable early precursor of the 3-O -methylmannose polysaccharides.
Reaction Schemes
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3,3'-di-O-methyl-4alpha-mannobiose
=
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1,3,3'-tri-O-methyl-4alpha-mannobiose
Synonyms
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3-O-methylmannose polysaccharide 1-O-methyltransferase
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S-adenosyl-L-methionine-dependent sugar 1-O-methyltransferase
MET1
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S-adenosyl-L-methionine-dependent sugar 1-O-methyltransferase
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S-adenosyl-L-methionine-dependent sugar 1-O-methyltransferase
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S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose = S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
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S-adenosyl-L-methionine:3,3'-di-O-methyl-4'-mannobiose 1-O-methyltransferase
Requires Mg2+. The enzyme, characterized from the bacterium Mycolicibacterium hassiacum, participates in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in nontuberculous mycobacteria. The methylation catalysed by this enzyme was shown to block the reducing end of 3,3'-di-O-methyl-alpha-mannobiose, a probable early precursor of the 3-O-methylmannose polysaccharides.
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S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
additional information
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S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
Substrates: -
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S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
Substrates: specific substrate
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S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
Substrates: -
?
S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
Substrates: specific substrate
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additional information
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Substrates: the enzyme is inactive against mannose, the unmethylated dimannoside alpha-1,4-mannobiose, or 3-O-methylmannose
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additional information
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Substrates: the enzyme is inactive against mannose, the unmethylated dimannoside alpha-1,4-mannobiose, or 3-O-methylmannose
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additional information
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Substrates: the enzyme is inactive against mannose, the unmethylated dimannoside alpha-1,4-mannobiose, or 3-O-methylmannose
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S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
Substrates: -
?
S-adenosyl-L-methionine + 3,3'-di-O-methyl-4alpha-mannobiose
S-adenosyl-L-homocysteine + 1,3,3'-tri-O-methyl-4alpha-mannobiose
Substrates: -
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Mg2+
required, 10 mM used in assay conditions
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EDTA
the recombinant enzyme is inactivated by 10 mM EDTA
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0.25 - 0.78
3,3'-di-O-methyl-4alpha-mannobiose
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0.055
S-adenosyl-L-methionine
at pH 7.5 and 37°C
0.25
3,3'-di-O-methyl-4alpha-mannobiose
wild type enzyme, at pH 7.5 and 37°C
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0.69
3,3'-di-O-methyl-4alpha-mannobiose
mutant enzyme E78A, at pH 7.5 and 37°C
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0.78
3,3'-di-O-methyl-4alpha-mannobiose
mutant enzyme H79A, at pH 7.5 and 37°C
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0.000033 - 0.00062
3,3'-di-O-methyl-4alpha-mannobiose
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0.000033
3,3'-di-O-methyl-4alpha-mannobiose
mutant enzyme E78A, at pH 7.5 and 37°C
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0.000033
3,3'-di-O-methyl-4alpha-mannobiose
mutant enzyme H79A, at pH 7.5 and 37°C
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0.00062
3,3'-di-O-methyl-4alpha-mannobiose
wild type enzyme, at pH 7.5 and 37°C
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0.00005 - 0.0025
3,3'-di-O-methyl-4alpha-mannobiose
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0.00005
3,3'-di-O-methyl-4alpha-mannobiose
mutant enzyme E78A, at pH 7.5 and 37°C
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0.00005
3,3'-di-O-methyl-4alpha-mannobiose
mutant enzyme H79A, at pH 7.5 and 37°C
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0.0025
3,3'-di-O-methyl-4alpha-mannobiose
wild type enzyme, at pH 7.5 and 37°C
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6.5 - 9.5
the enzyme is active between pH 6.5 and 9.5
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
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Cell Line Links
Gene Links
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MET1_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
218
0
23890
Swiss-Prot
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in complex with S-adenosyl-L-homocysteine, sitting drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.5, 0.2 M MgCl2, 20% (w/v) PEG 8000 or 0.1 M MES pH 6.5, and 1.6 M MgSO4
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E78A
the mutant shows about 10% activity compared to the wild type enzyme
H79A
the mutant shows about 13% activity compared to the wild type enzyme
E78A
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the mutant shows about 10% activity compared to the wild type enzyme
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H79A
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the mutant shows about 13% activity compared to the wild type enzyme
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HisTrap column chromatography
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expressed as His-tagged recombinant protein in Escherichia coli BL21(DE3) cells
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Ripoll-Rozada, J.; Costa, M.; Manso, J.A.; Maranha, A.; Miranda, V.; Sequeira, A.; Ventura, M.R.; Macedo-Ribeiro, S.; Pereira, P.J.B.; Empadinhas, N.
Biosynthesis of mycobacterial methylmannose polysaccharides requires a unique 1-O-methyltransferase specific for 3-O-methylated mannosides
Proc. Natl. Acad. Sci. USA
116
835-844
2019
Mycolicibacterium hassiacum (K5B7F3), Mycolicibacterium hassiacum, Mycolicibacterium hassiacum DSM 44199 (K5B7F3)
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