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Literature summary for 5.1.3.2 extracted from

  • Majumdar, S.; Ghatak, J.; Mukherji, S.; Bhattacharjee, H.; Bhaduri, A.
    UDPgalactose 4-epimerase from Saccharomyces cerevisiae. A bifunctional enzyme with aldose 1-epimerase activity (2004), Eur. J. Biochem., 271, 753-759.
    View publication on PubMed
Search for more literature for 5.1.3.2

Cloned(Commentary)

Cloned (Comment) Organism
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 Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
5'-UMP epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose Saccharomyces cerevisiae
L-arabinose epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The epimerase and mutarotase activities are located in different regions of the epimerase holoenzyme Saccharomyces cerevisiae ?
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 ?