Literature summary for 2.1.1.237 extracted from

Bernard, S.M.; Akey, D.L.; Tripathi, A.; Park, S.R.; Konwerski, J.R.; Anzai, Y.; Li, S.; Kato, F.; Sherman, D.H.; Smith, J.L.
Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases (2015), ACS Chem. Biol., 10, 1340-1351.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of crystal structures of MycF, including the free enzyme and complexes with S-adenosyl homocysteine, substrate, product, and unnatural substrates	Micromonospora griseorubida

Protein Variants

Protein Variants	Comment	Organism
additional information	a single amino acid substitution relaxes the 2'-methoxy specificity but retains regiospecificity. The engineered variant produces a new mycinamicin analogue, demonstrating the utility of structural information to facilitate bioengineering approaches for the chemoenzymatic synthesis of complex small molecules containing modified sugars	Micromonospora griseorubida

Organism

Organism	UniProt	Comment	Textmining
Micromonospora griseorubida	Q49492	-	-

Synonyms

Synonyms	Comment	Organism
MycF	-	Micromonospora griseorubida

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	cofacor binding induces substantial ordering that creates the binding site for the natural substrate, and a bound metal ion positions the substrate for catalysis	Micromonospora griseorubida

General Information

General Information	Comment	Organism
evolution	structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases, overview	Micromonospora griseorubida
metabolism	the 3'-O-methyltransferase enzyme is involved in the biosynthesis of the macrolide antibiotic mycinamicin	Micromonospora griseorubida
additional information	using the MycF substrate complex and the modeled substrate complex of a 4'-specific homologue, active site residues were identified that correlate with the 3' or 4' specificity of MycF family members and define the protein and substrate features that direct the regiochemistry of methyltransfer	Micromonospora griseorubida
physiological function	S-adenosyl-L-methionine cofacor binding induces substantial ordering that creates the binding site for the natural substrate, and a bound metal ion positions the substrate for catalysis	Micromonospora griseorubida

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Release 2023.1 (January 2023)