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Literature summary for 5.1.3.32 extracted from

  • 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 (2005), J. Mol. Biol., 349, 153-162.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli

Protein Variants

Protein Variants Comment Organism
H22A mutant does not fold properly Escherichia coli
H22K mutant does not fold properly Escherichia coli
Y18A mutant does not fold properly Escherichia coli
Y18E mutant does not fold properly Escherichia coli
Y18F binding affinity for L-rhamnose is comparable to that of the wild-type, no catalytic activity Escherichia coli
Y18H mutant does not fold properly Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P32156
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General Information

General Information Comment Organism
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 Escherichia coli