Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Carney, A.E.; Holden, H.M.
    Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose (2011), Biochemistry, 50, 780-787.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.1.1.235 medicine the enzyme is involved in biosynthesis of D-mycaminose. D-Mycaminose is an unusual dideoxy sugar found attached to the antibiotic tylosin, a commonly used veterinarian therapeutic Streptomyces fradiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.235 expression in Escherichia coli Streptomyces fradiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.235 hanging drop method of vapor diffusion method, high resolution X-ray structures of TylM1, one in which the enzyme contains bound SAM and dTDP-phenol and the second in which the protein is complexed with S-adenosyl-L-homocysteine and dTDP-3-amino-3,6-dideoxyglucose, its natural substrate. Combined, these two structures, solved to 1.35 A and 1.79 A resolution, respectively, show the orientations of SAM and the dTDP-linked sugar substrate within the active site region. Specifically, the C-30 amino group of the hexose is in the correct position for an in-line attack at the reactive methyl group of S-adenosyl-L-methionine. High-resolution X-ray models show that the observed perturbations in the kinetic constants of the mutant enzynes H123A and H123N are not due to major changes in their threedimensional folds. Most likely the proton on the C-3' amino group is transferred to one of the water molecules lining the active site pocket as catalysis proceeds Streptomyces fradiae

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.235 H123A mutant protein retains catalytic activity, the kcat/Km is reduced to 1.8% compared to the wild-type enzyme Streptomyces fradiae
2.1.1.235 H123N mutant protein retains catalytic activity, the kcat/Km is reduced to 0.37% compared to the wild-type enzyme Streptomyces fradiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.235 0.045
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, wild-type enzyme Streptomyces fradiae
2.1.1.235 0.67
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, mutant enzyme H123A Streptomyces fradiae
2.1.1.235 0.93
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, mutant enzyme H123N Streptomyces fradiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.235 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose Streptomyces fradiae the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.235 Streptomyces fradiae P95748
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.235
-
 Streptomyces fradiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.235 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
-
 ?
2.1.1.235 2 S-adenosyl-L-methionine + dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar Streptomyces fradiae 2 S-adenosyl-L-homocysteine + dTDP-3-dimethylamino-3,6-dideoxy-alpha-D-glucopyranose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.235 TylM1
-
 Streptomyces fradiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.235 37
-
 assay at Streptomyces fradiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.235 0.0126
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, mutant enzyme H123N Streptomyces fradiae
2.1.1.235 0.046
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, mutant enzyme H123A Streptomyces fradiae
2.1.1.235 0.172
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, wild-type enzyme Streptomyces fradiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.235 8.5
-
 assay at Streptomyces fradiae

General Information

EC Number General Information Comment Organism
2.1.1.235 physiological function the enzyme is involved in biosynthesis of D-mycaminose. It is synthesized by the Gram-positive bacterium Streptomyces fradiae as a dTDP-linked sugar Streptomyces fradiae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.235 0.0135
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, mutant enzyme H123N Streptomyces fradiae
2.1.1.235 0.069
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, mutant enzyme H123A Streptomyces fradiae
2.1.1.235 3.8
-
 dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose pH 8.5, 37°C, wild-type enzyme Streptomyces fradiae