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
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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
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Reaction
Reaction on EC 5.1.3.3 - Aldose 1-epimerase
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the mechanism of the enzymatically catalyzed mutarotation is basically different from that of the nonenzymatically catalyzed mutarotation. The mutarotase acts primarily as a base catalyst. The enzymatically catalyzed mutarotation proceeds via the acyclic aldehyde form of the aldose
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alpha-D-glucose = beta-D-glucose
Trp is involved as glucose-binding site and catalysis of the mutarotation reaction is accomplished by a ring-distortion type of mechanism
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alpha-D-glucose = beta-D-glucose
reaction mechanism does not involve dehydration, any dehydrogenation reaction on carbon-bound hydrogen, or the hydrated derivative of glucose aldehyde, nor is a single displacement mechanism involved. The enzyme-catalyzed mutarotation is essentially similar to the spontaneous or acid catalyzed process. Mutarotase is an enzyme with a proton-transferring function #2#
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alpha-D-glucose = beta-D-glucose
concerted general acid/general base mechanism
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alpha-D-glucose = beta-D-glucose
E307 and H176 may act as catalytic acid and catalytic base, respectively
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alpha-D-glucose = beta-D-glucose
mechanism, one of the catalytic groups H104, H175, or E309, shuttles a proton to and from the endocyclic oxygen and the other two shuttle protons to the anomeric oxygen atoms. Ring opening of alpha-D-glucose limits the rate at low pH, but ring closure does not become rate limiting at pH up to 8.5
alpha-D-glucose = beta-D-glucose
residues E304 and H170 are critical for catalysis and H96 and D243 are important for substrate positioning
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alpha-D-glucose = beta-D-glucose
residues responsible for anchoring the sugar include R71, H96, H170, D243 and E304. E304 may act as general acid/base
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