Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages and are released in alpha form during degradation. This enzyme accelerates maturotation to the beta form via the open form (which also occurs as a slow spontaneous reaction). The open form is necessary for further metabolism by the bacteria.
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The enzyme appears in viruses and cellular organisms
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SYSTEMATIC NAME
IUBMB Comments
N-acetyl-alpha-neuraminate 2-epimerase
Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages and are released in alpha form during degradation. This enzyme accelerates maturotation to the beta form via the open form (which also occurs as a slow spontaneous reaction). The open form is necessary for further metabolism by the bacteria.
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in he beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses
the mutant of YjhT is severely impaired in its ability to enhance the mutarotation rate above the spontaneous rate. Circular dichroism spectrum of the mutant is indistinguishable from that of the wild-type protein, suggesting that the phenotype is not because of misfolding of YjhT
mutant shows a decreased but observable activity. Circular dichroism spectrum of the mutant is indistinguishable from that of the wild-type protein, suggesting that the phenotype is not because of misfolding of YjhT
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History
5.1.3.24 N-acetylneuraminate epimerase
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