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

BRENDA support

Literature summary for 1.14.13.180 extracted from

  • Lindqvist, Y.; Koskiniemi, H.; Jansson, A.; Sandalova, T.; Schnell, R.; Liu, Z.; Mäntsälä, P.; Niemi, J.; Schneider, G.
    Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis (2009), J. Mol. Biol., 393, 966-977.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of a ternary complex of this enzyme from Streptomyces purpurascens, RdmE, with FAD and the substrate aklavinone Streptomyces purpurascens

Protein Variants

Protein Variants Comment Organism
R373X mutants at position Arg373 retain catalytic activity close to wild-type level Streptomyces purpurascens
Y224F inactive mutant enzyme Streptomyces purpurascens

Organism

Organism UniProt Comment Textmining
Streptomyces purpurascens Q54530
-
-

Synonyms

Synonyms Comment Organism
RdmE
-
Streptomyces purpurascens

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme contains a FAD-binding domain Streptomyces purpurascens