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Literature summary for 3.5.1.108 extracted from

  • Gattis, S.G.; Hernick, M.; Fierke, C.A.
    Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions (2010), J. Biol. Chem., 285, 33788-33796.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the metal bound to LpxC purified from Escherichia coli grown in minimal medium is mainly Fe(II). However, the ratio of iron/zinc bound to LpxC varies with the metal content of the medium. Fe(II) is the thermodynamically favored metal cofactor for LpxC under cellular conditions, but the metal cofactor in LpxC can switch between iron and zinc in response to perturbations in available metal ions Escherichia coli
Zn2+ the metal bound to LpxC purified from Escherichia coli grown in minimal medium is mainly Fe(II). However, the ratio of iron/zinc bound to LpxC varies with the metal content of the medium. The metal cofactor in LpxC can switch between iron and zinc in response to perturbations in available metal ions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Purification (Commentary)

Purification (Comment) Organism
pulldown method to rapidly purify tagged LpxC under anaerobic conditions Escherichia coli