2,7-anhydro-N-acetylneuraminate hydratase [Escherichia coli str. K-12 - Protein

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The putative Escherichia coli dehydrogenase YjhC metabolises two dehydrated forms of N-acetylneuraminate produced by some sialidases. [Biosci Rep. 2020]
The putative Escherichia coli dehydrogenase YjhC metabolises two dehydrated forms of N-acetylneuraminate produced by some sialidases.
Kentache T, Thabault L, Peracchi A, Frédérick R, Bommer GT, Van Schaftingen E. Biosci Rep. 2020 Jun 26; 40(6).
On the structure and function of Escherichia coli YjhC: An oxidoreductase involved in bacterial sialic acid metabolism. [Proteins. 2020]
On the structure and function of Escherichia coli YjhC: An oxidoreductase involved in bacterial sialic acid metabolism.
Horne CR, Kind L, Davies JS, Dobson RCJ. Proteins. 2020 May; 88(5):654-668. Epub 2019 Nov 21.
Distant cis-active sequences and sialic acid control the expression of fimB in Escherichia coli K-12. [Mol Microbiol. 2003]
Distant cis-active sequences and sialic acid control the expression of fimB in Escherichia coli K-12.
El-Labany S, Sohanpal BK, Lahooti M, Akerman R, Blomfield IC. Mol Microbiol. 2003 Aug; 49(4):1109-18.

KpLE2 phage-like element; 2,7-anhydro-N-acetylneuraminate hydratase [BioCyc]
KpLE2 phage-like element; 2,7-anhydro-N-acetylneuraminate hydratase
BioCyc
Transcript/Protein Information [PANTHER Classification System]
Transcript/Protein Information
PANTHER Classification System

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