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Literature summary for 5.4.99.9 extracted from

  • Yao, X.; Bleile, D.; Yuan, Y.; Chao, J.; Sarathy, K.; Sanders, D.; Pinto, B.; O’Neill, M.
    Substrate directs enzyme dynamics by bridging distal sites: UDP-galactopyranose mutase (2009), Proteins Struct. Funct. Bioinform., 74, 972-979.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Klebsiella pneumoniae

Protein Variants

Protein Variants Comment Organism
W160A redox-switched binding affinity of substrate reverses in the W160A mutant where it only binds when oxidized Klebsiella pneumoniae
W70F/W290F the double mutant binds substrate in a similar manner to wild type and has comparable enzyme activity (90%) Klebsiella pneumoniae

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Klebsiella pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-galactopyranose
-
Klebsiella pneumoniae UDP-galactofuranose
-
r

Synonyms

Synonyms Comment Organism
UGM
-
Klebsiella pneumoniae

Cofactor

Cofactor Comment Organism Structure
FAD flavoenzyme, activity depends on FAD redox state Klebsiella pneumoniae