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Literature summary for 5.1.3.24 extracted from

  • Severi, E.; Müller, A.; Potts, J.R.; Leech, A.; Williamson, D.; Wilson, K.S.; Thomas, G.H.
    Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT (2008), J. Biol. Chem., 283, 4841-4849.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
vapor diffusion method, 1.5 A resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
E209A 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 Escherichia coli
E325A mutation has no effect on the activity Escherichia coli
H278A mutation has no effect on the activity Escherichia coli
K11A mutation has no effect on the activity Escherichia coli
K283A mutation has no effect on the activity Escherichia coli
R215A 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 Escherichia coli
Y309A mutation has no effect on the activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Escherichia coli
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38685
-
2 * 38685, electrospray mass spectrometry Escherichia coli
73900
-
equilibrium sedimentation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-alpha-neuraminate Escherichia coli 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 N-acetyl-beta-neuraminate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P39371
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-alpha-neuraminate 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 Escherichia coli N-acetyl-beta-neuraminate
-
?
N-acetyl-alpha-neuraminate the enzyme converts alpha-N-acetylneuranimic acid to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers Escherichia coli N-acetyl-beta-neuraminate
-
?

Subunits

Subunits Comment Organism
dimer 2 * 38685, electrospray mass spectrometry Escherichia coli

Synonyms

Synonyms Comment Organism
N-acetylneuraminate mutarotase
-
Escherichia coli
sialic acid epimerase
-
Escherichia coli
YjhT
-
Escherichia coli

General Information

General Information Comment Organism
physiological function 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 Escherichia coli