5.1.3.3: Aldose 1-epimerase
This is an abbreviated version!
For detailed information about Aldose 1-epimerase, go to the full flat file.
Word Map on EC 5.1.3.3
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5.1.3.3
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anomer
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mutarotation
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leloir
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beta-anomers
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alpha-d-galactose
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beta-d-galactose
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galactokinase
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alpha-d-glucose
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gale
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analysis
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synthesis
- 5.1.3.3
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anomer
-
mutarotation
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leloir
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beta-anomers
- alpha-d-galactose
- beta-d-galactose
- galactokinase
- alpha-d-glucose
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gale
- analysis
- synthesis
Reaction
Synonyms
aldose 1-epimerase, aldose 1-epimerase-like protein, aldose mutarotase, aldose-1-epimerase, aldose-l-epimerase, Epimerase, aldose-1, Gal10p, galactomutarotase, galactose mutarotase, galactose mutarotase/UDP-galactose 4-epimerase protein, GalM, Mutarotase, mutarotase YeaD, NbAELP, stYeaD, YeaD
ECTree
5.1.3.3 Aldose 1-epimeraseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 5.1.3.3 - Aldose 1-epimerase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-D-Fructose
alpha-D-Fructose
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135% of the activity relative to alpha-D-glucose
-
?
alpha-D-galactose
beta-D-galactose
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105% of the activity relative to alpha-D-glucose
-
-
?
alpha-D-galactose
beta-D-galactose
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6% of the activity with alpha-D-glucose
-
-
?
alpha-D-galactose
beta-D-galactose
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the two enzyme activities, galactose mutarotase and UDP-galactose 4-epimerase, are required for the Leloir pathway of D-galactose catabolism, they are contained within a single proteinGal10p
-
-
?
alpha-D-galactose
beta-D-galactose
-
the simultaneous epimerase and the mutarotase activities of the bifunctional enzyme do not affect each other, the mutarotase active site has a strong preference for galactose over glucose, overview
-
-
?
alpha-D-glucose
beta-D-glucose
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the simultaneous epimerase and the mutarotase activities of the bifunctional enzyme do not affect each other, the mutarotase active site has a strong preference for galactose over glucose, overview
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-
?
alpha-D-Glycero-D-galactoheptopyranose
beta-D-Glycero-D-galactoheptopyranose
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-
-
?
alpha-D-Glycero-D-galactoheptopyranose
beta-D-Glycero-D-galactoheptopyranose
-
-
-
-
?
alpha-D-xylose
beta-D-xylose
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31% of the activity relative to alpha-D-glucose
-
-
?
alpha-D-xylose
beta-D-xylose
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23% of the activity with alpha-D-glucose
-
-
?
alpha-L-arabinose
beta-L-arabinose
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beta-L-arabinose is epimerized at 108% of the activity relative to alpha-D-glucose
-
-
?
beta-Lactose
alpha-Lactose
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10% of the activity relative to alpha-D-glucose
-
?
beta-Maltose
alpha-Maltose
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13% of the activity relative to alpha-D-glucose
-
?
additional information
?
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key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha-anomer and beta-anomer of hexose sugars such as glucose and galactose
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?
additional information
?
-
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key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha-anomer and beta-anomer of hexose sugars such as glucose and galactose
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?
additional information
?
-
-
may be involved in the metabolism of D-glucose in nuclei
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-
?
additional information
?
-
-
glucose is most probably not the best physiological substrate of the enzyme
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-
?
additional information
?
-
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identification of residues involved in catalysis and substrate binding, role of Arg74 and Arg99, found only in YeaD-like proteins, in ligand anchoring, the specificity of YeaD is different from those of galactose mutarotase, overview
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-
?
