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Literature summary for 5.4.99.9 extracted from

  • Karunan Partha, S.; Bonderoff, S.A.; van Straaten, K.E.; Sanders, D.A.
    Expression, purification and preliminary X-ray crystallographic analysis of UDP-galactopyranose mutase from Deinococcus radiodurans (2009), Acta Crystallogr. Sect. F, 65, 843-845.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.99.9

Cloned(Commentary)

Cloned (Comment) Organism
-
 Deinococcus radiodurans

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with UDP-galactopyranose, microbatch-under-oil method, using 0.1 M HEPES pH 7.0, 0.2 M LiCl, and 20% (w/v) PEG 6000 Deinococcus radiodurans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-galactopyranose Deinococcus radiodurans
-
 UDP-galactofuranose
-
 r

Organism

Organism UniProt Comment Textmining
Deinococcus radiodurans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HQ20 column chromatography and HP-20 hydrophobic interaction chromatography column Deinococcus radiodurans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-galactopyranose
-
 Deinococcus radiodurans UDP-galactofuranose
-
 r

Synonyms

Synonyms Comment Organism
UGM
-
 Deinococcus radiodurans

Cofactor

Cofactor Comment Organism Structure
FAD UGM is only catalytically active when the flavin is in the reduced form Deinococcus radiodurans