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

BRENDA support

Literature summary for 2.1.1.292 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)

Cloned (Comment) Organism
-
Streptomyces peucetius

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Organism

Organism UniProt Comment Textmining
Streptomyces peucetius Q06528
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptomyces peucetius

Subunits

Subunits Comment Organism
homodimer
-
Streptomyces peucetius

Synonyms

Synonyms Comment Organism
DnrK
-
Streptomyces peucetius

General Information

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