Any feedback?
Literature summary for 3.5.1.108 extracted from
- Molecular recognition by Escherichia coli UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase is modulated by bound metal ions (2006), Biochemistry, 45, 14573-14581.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | this enzyme catalyzes a committed step in the biosynthesis of lipid A, and for this reason, LpxC is a target for the development of antibiotics in the treatment of Gram-negative bacterial infections | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the affinity of LpxC for both product and fatty acids is significantly influenced by changes in the number and identity of metal ions bound to the LpxC active site. Therefore, interactions with these metal ions are critical for molecular recognition of ligands by LpxC and may mimic similar contacts with active site inhibitors. These data indicate that the potency of LpxC inhibitors in vitro can be altered by assay conditions used in screening and/or development of LpxC inhibitors and that the metal ion status of LpxC in vivo will likely influence the effectiveness of LpxC inhibitors as antibiotics | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | Escherichia coli | committed step in the biosynthesis of lipid A | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | - |
Escherichia coli | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? | |
| UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O | committed step in the biosynthesis of lipid A | Escherichia coli | UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase | - |
Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
