Literature summary for 2.1.1.235 extracted from

Fick, R.J.; Horowitz, S.; McDole, B.G.; Clay, M.C.; Mehl, R.A.; Al-Hashimi, H.M.; Scheiner, S.; Trievel, R.C.
Structural and functional characterization of sulfonium carbon-oxygen hydrogen bonding in the deoxyamino sugar methyltransferase TylM1 (2019), Biochemistry, 58, 2152-2159 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme TylM1 mutants Y14F, Y14pAF, and S120A in complex with SAH and dTDP-phenol, X-ray diffraction structure determination and analysis at 1.37-1.78 A resolution	Streptomyces fradiae

Protein Variants

Protein Variants	Comment	Organism
S120A	site-directed mutagenesis, the mutant exhibits a modest decrease in its catalytic efficiency compared to wild-type	Streptomyces fradiae
Y14F	site-directed mutagenesis, the mutation results in an approximately 30fold decrease in catalytic efficiency compared to wild-type	Streptomyces fradiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetic analysis of wild-type enzyme and mutants	Streptomyces fradiae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose	Streptomyces fradiae	-	2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces fradiae	P95748	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose	-	Streptomyces fradiae	2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose	-	?

Synonyms

Synonyms	Comment	Organism
deoxyamino sugar methyltransferase	-	Streptomyces fradiae
N-methyltransferase	-	Streptomyces fradiae
TylM1	-	Streptomyces fradiae

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Streptomyces fradiae

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Streptomyces fradiae

General Information

General Information	Comment	Organism
additional information	active site structures of WT TylM1 and the Tyr14 and Ser120 mutants, structure modeling, overview. Quantum mechanical calculations of the activation barrier energies of wild-type TylM1 and the Tyr14 mutants suggest that substitutions which abrogate hydrogen bonding with the AdoMet methyl group impair methyl transfer	Streptomyces fradiae
physiological function	CH-O hydrogen bonding play roles in modulating the catalytic efficiency of TylM1	Streptomyces fradiae

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Release 2023.1 (January 2023)