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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
rhamnose 1-epimerase, RhaU, type-3 mutarotase, YiiL,
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alpha-L-rhamnopyranose = beta-L-rhamnopyranose
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L-rhamnopyranose 1-epimerase
The enzyme is specific for L-rhamnopyranose.
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alpha-L-rhamnopyranose
beta-L-rhamnopyranose
alpha-L-rhamnopyranose
beta-L-rhamnopyranose
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alpha-L-rhamnopyranose
beta-L-rhamnopyranose
the enzyme is specific for L-rhamnopyranose
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alpha-L-rhamnopyranose
beta-L-rhamnopyranose
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SwissProt
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UniProt
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physiological function
gene deletion leads o decreased growth rate only in the presence of low concentrations of L-rhamnose, with no difference in growth rate between the wild-type and mutant strains when the concentration of L-rhamnose in the media is 0.2%. The maximum amount of growth and the lag phase time of the wild-type strain are higher and shorter, respectively, compared with those of the mutant
physiological function
growth phenotype on L-rhamnose of a a gene deletion strain is slower than that of the wild-type strain, although the ultimate cell yields are equivalent. The transport of L-rhamnose into the cell and the rate of its phosphorylation are unaffected by the deletion
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12000
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
14000
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
16595
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
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dimer
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
additional information
the enzyme seems to require multimeric or dimeric structure for their enzymatic activity
additional information
mass spectrometry hows that enzyme exists predominantly as a dimer and that increasing ionization voltage causes its dissociation to a monomer
additional information
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mass spectrometry hows that enzyme exists predominantly as a dimer and that increasing ionization voltage causes its dissociation to a monomer
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in complex with L-rhamnose, to 1.8 A resolution. Protein is a locally asymmetric dimer and has a preference for the beta-form of L-rhamnose
to 1.6 A resolution. Structure shows a dimer in the asymmetric unit with a very similar structure to that of L-rhamnose mutarotase YiiL of Escherichia coli
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H22A
mutant does not fold properly
H22K
mutant does not fold properly
Y18A
mutant does not fold properly
Y18E
mutant does not fold properly
Y18F
binding affinity for L-rhamnose is comparable to that of the wild-type, no catalytic activity
Y18H
mutant does not fold properly
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expresssion in Escherichia coli
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Ryu, K.S.; Kim, C.; Kim, I.; Yoo, S.; Choi, B.S.; Park, C.
NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration
J. Biol. Chem.
279
25544-25548
2004
Escherichia coli (P32156)
brenda
Richardson, J.S.; Carpena, X.; Switala, J.; Perez-Luque, R.; Donald, L.J.; Loewen, P.C.; Oresnik, I.J.
RhaU of Rhizobium leguminosarum is a rhamnose mutarotase
J. Bacteriol.
190
2903-2910
2008
Rhizobium leguminosarum (Q7BSH1), Rhizobium leguminosarum
brenda
Ryu, K.S.; Kim, J.I.; Cho, S.J.; Park, D.; Park, C.; Cheong, H.K.; Lee, J.O.; Choi, B.S.
Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase
J. Mol. Biol.
349
153-162
2005
Escherichia coli (P32156)
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5.1.3.32 L-rhamnose mutarotase
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