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Literature summary for 2.4.1.182 extracted from
- Structure, inhibition, and regulation of essential lipid A enzymes (2017), Biochim. Biophys. Acta, 1862, 1424-1438 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | LpxB catalysis requires the presence of detergents | Escherichia coli | |
| additional information | LpxB catalysis requires the presence of detergents | Chlamydia trachomatis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene lpxB, recombinant overexpression of LpxB in Escherichia coli resulting in the accumulation of aberrant tubular membranes of a uniform diameter along the inner surface of the bacterial inner membrane, suggesting that the accumulation of the lipid product of the LpxB reaction, 2',3'-diacylglucosamine-(beta,1'-6)-2,3-diacylglucosamine-1-phosphate (DSMP), is toxic to cells | Chlamydia trachomatis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | LpxB is a membrane-associated lipid A enzyme | Escherichia coli | 16020 | - |
| membrane | LpxB is a membrane-associated lipid A enzyme | Chlamydia trachomatis | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | Escherichia coli | - |
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
? |  |
| UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | Chlamydia trachomatis | - |
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
? | |
| UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | Chlamydia trachomatis D/UW-3/Cx | - |
UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Chlamydia trachomatis | O84416 | - |
- |
| Chlamydia trachomatis D/UW-3/Cx | O84416 | - |
- |
| Escherichia coli | P10441 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
Escherichia coli | UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
? | |
| UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
Chlamydia trachomatis | UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
? | |
| UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
Chlamydia trachomatis D/UW-3/Cx | UDP + 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-beta-D-glucosaminyl-(1->6)-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| lipid A disaccharide synthetase | - |
Escherichia coli |
| lipid A disaccharide synthetase | - |
Chlamydia trachomatis |
| LpxB | - |
Escherichia coli |
| LpxB | - |
Chlamydia trachomatis |
| pgsB | - |
Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
LpxB is most active at neutral pH | Escherichia coli |
| additional information | - |
LpxB is most active at neutral pH | Chlamydia trachomatis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | LpxB is an inverting glycosyltransferase of family 19 of the GT-B superfamily | Escherichia coli |
| evolution | LpxB is an inverting glycosyltransferase of family 19 of the GT-B superfamily | Chlamydia trachomatis |
| malfunction | overexpression of LpxB in Escherichia coli results in the accumulation of aberrant tubular membranes of a uniform diameter along the inner surface of the bacterial inner membrane, suggesting that the accumulation of the lipid product of the LpxB reaction, 2',3'-diacylglucosamine-(beta,1'-6)-2,3-diacylglucosamine-1-phosphate (DSMP), is toxic to cells | Chlamydia trachomatis |
| physiological function | role of LpxB as the disaccharide synthetase to condense UDP-DAGn with lipid X to form DSMP and UDP | Escherichia coli |
| physiological function | role of LpxB as the disaccharide synthetase to condense UDP-DAGn with lipid X to form DSMP and UDP | Chlamydia trachomatis |
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