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Literature summary extracted from

  • Jansson, A.; Koskiniemi, H.; Mäntsälä, P.; Niemi, J.; Schneider, G.
    Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products (2004), J. Biol. Chem., 279, 41149-41156.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.292
-
Streptomyces peucetius

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.292 the crystal structure of the ternary complex of this enzyme with the bound products S-adenosyl-L-homocysteine and 4-methoxy-epsilon-rhodomycin T is determined to a 2.35 A resolution, vapor diffusion method at 20°C Streptomyces peucetius

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.292 Y142W 48% of the rate of the recombinant native enzyme with 4-methoxy-epsilon-rhodomycin T Streptomyces peucetius

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.292 Streptomyces peucetius Q06528
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.292
-
Streptomyces peucetius

Subunits

EC Number Subunits Comment Organism
2.1.1.292 homodimer
-
Streptomyces peucetius

Synonyms

EC Number Synonyms Comment Organism
2.1.1.292 DnrK
-
Streptomyces peucetius

General Information

EC Number General Information Comment Organism
2.1.1.292 physiological function the enzyme is involved in daunorubicin biosynthesis Streptomyces peucetius