EC number:2.1.1.101

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.101
Description:Macrocin O-methyltransferase.
Alternative Name: MOMT.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.101
BRENDA Enzyme Link: BRENDA 2.1.1.101
KEGG Enzyme Link: KEGG2.1.1.101
BioCyc Enzyme Link: BioCyc 2.1.1.101
ExPASy Enzyme Link: ExPASy2.1.1.101
EC2PDB Enzyme Link: EC2PDB 2.1.1.101
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.101
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.101
IntEnz Enzyme Link: IntEnz 2.1.1.101
MEDLINE Enzyme Link: MEDLINE 2.1.1.101

EC number:2.1.1.101

MSA:

2.1.1.101;
Phylogenetic Tree:

2.1.1.101;
Uniprot:
M-CSA:
RHEA:17269 macrocin + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + tylosin
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cloning genes for the biosynthesis of a macrolide antibiotic.Fishman SE, Cox K, Larson JL, Reynolds PA, Seno ET, Yeh WK, Van Frank R, Hershberger CL1987 Dec3479787
Two distinctive O-methyltransferases catalyzing penultimate and terminal reactions of macrolide antibiotic (tylosin) biosynthesis. Substrate specificity, enzyme inhibition, and kinetic mechanism.Kreuzman AJ, Turner JR, Yeh WK1988 Oct 253170602
Purification, characterization, and kinetic mechanism of S-adenosyl-L-methionine:macrocin O-methyltransferase from Streptomyces fradiae.Bauer NJ, Kreuzman AJ, Dotzlaf JE, Yeh WK1988 Oct 253170601