| ID Source | ID |
|---|---|
| PubMed CID | 449223 |
| CHEMBL ID | 1236446 |
| MeSH ID | M0473390 |
| Synonym |
|---|
| CHEMBL1236446 , |
| 1,5-anhydro-2-c-(carboxymethyl-n-hydroxyamide)-2-deoxy-3-o-myristoyl-d-glucitol |
| tux , |
| tu-514 |
| 1XXE |
| 2GO4 |
| DB01991 |
| [(2r,3s,4r,5s)-3-hydroxy-5-[2-(hydroxyamino)-2-oxoethyl]-2-(hydroxymethyl)oxan-4-yl] tetradecanoate |
| bdbm50483375 |
| 1,5-anhydro-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-3-o-tetradecanoyl-d-glucitol |
| Q27466758 |
| Protein | Taxonomy | Measurement | Average | Min (ref.) | Avg (ref.) | Max (ref.) | Bioassay(s) |
|---|---|---|---|---|---|---|---|
| Chain A, UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase | Aquifex aeolicus | Ki | 3.9000 | 3.9000 | 3.9000 | 3.9000 | AID977610 |
| Chain A, UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase | Aquifex aeolicus | IC50 (µMol) | 7.0000 | 7.0000 | 7.0000 | 7.0000 | AID977608 |
| UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 | Ki | 0.6500 | 0.0001 | 0.0880 | 0.6500 | AID568324; AID652927 |
| [prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023] | |||||||
| Process | via Protein(s) | Taxonomy |
|---|---|---|
| lipid A biosynthetic process | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| phosphate-containing compound metabolic process | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| lipid A biosynthetic process | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| organophosphate metabolic process | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| carbohydrate derivative metabolic process | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| [Information is prepared from geneontology information from the June-17-2024 release] | ||
| Process | via Protein(s) | Taxonomy |
|---|---|---|
| iron ion binding | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| zinc ion binding | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| hydrolase activity | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| deacetylase activity | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| metal ion binding | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| UDP-3-O-acyl-N-acetylglucosamine deacetylase activity | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| [Information is prepared from geneontology information from the June-17-2024 release] | ||
| Process | via Protein(s) | Taxonomy |
|---|---|---|
| cytoplasm | UDP-3-O-acyl-N-acetylglucosamine deacetylase | Escherichia coli K-12 |
| [Information is prepared from geneontology information from the June-17-2024 release] | ||
| Assay ID | Title | Year | Journal | Article |
|---|---|---|---|---|
| AID1811 | Experimentally measured binding affinity data derived from PDB | 2005 | Biochemistry, Feb-01, Volume: 44, Issue:4 | Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design. |
| AID977610 | Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB | 2005 | Biochemistry, Feb-01, Volume: 44, Issue:4 | Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design. |
| AID568324 | Inhibition of Escherichia coli LpxC | 2011 | Bioorganic & medicinal chemistry letters, Feb-15, Volume: 21, Issue:4 | Design and synthesis of potent Gram-negative specific LpxC inhibitors. |
| AID652927 | Inhibition of Escherichia coli LpxC | 2012 | Bioorganic & medicinal chemistry letters, Apr-01, Volume: 22, Issue:7 | Structure based design of an in vivo active hydroxamic acid inhibitor of P. aeruginosa LpxC. |
| AID977608 | Experimentally measured binding affinity data (IC50) for protein-ligand complexes derived from PDB | 2006 | Biochemistry, Jul-04, Volume: 45, Issue:26 | Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase. |
| AID1811 | Experimentally measured binding affinity data derived from PDB | 2006 | Biochemistry, Jul-04, Volume: 45, Issue:26 | Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase. |
| [information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] | ||||
| Timeframe | Studies, This Drug (%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (60.00) | 29.6817 |
| 2010's | 2 (40.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| [information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023] | ||
According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be strong demand-to-supply ratio for research on this compound.
| This Compound (45.53) All Compounds (24.57) |
| Publication Type | This drug (%) | All Drugs (%) |
|---|---|---|
| Trials | 0 (0.00%) | 5.53% |
| Reviews | 0 (0.00%) | 6.00% |
| Case Studies | 0 (0.00%) | 4.05% |
| Observational | 0 (0.00%) | 0.25% |
| Other | 5 (100.00%) | 84.16% |
| [information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023] | ||