Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | the substrate preferentially coordinates to the active site Zn2+ via its carbonyl oxygen between a Zn2+-bound H2O and an adjacent threonine. Furthermore, upon substrate binding a nearby Glu78 residue is found to readily deprotonate the remaining Zn2+-bound H2O | Aquifex aeolicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | Aquifex aeolicus | LpxC is a key enzyme in the biochemical synthesis of Lipid A | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
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Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | LpxC is a key enzyme in the biochemical synthesis of Lipid A | Aquifex aeolicus | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? | |
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | the mechanism of LpxC proceeds via four steps: (1) initial hydroxylation of the substrates carbonyl carbon to give a gem-diolate intermediate, (2) protonation of the amide nitrogen by the histidine His265-H+, (3) a barrier-less change in the active site-intermediate hydrogen-bond network and finally, (4) C-N bond cleavage. The rate-determining step of the mechanism of LpxC is the initial hydroxylation while the final C-N bond cleavage occurs with an overall barrier of 23.6 kJ/mol. LpxC uses a general acid/base pair mechanism as indicated by the fact that both His265-H+ and Glu78 are accordingly involved | Aquifex aeolicus | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
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Synonyms | Comment | Organism |
---|---|---|
LpxC | - |
Aquifex aeolicus |