EC Number | Cloned (Comment) | Organism |
---|---|---|
3.6.1.54 | expressed in lpxh-deficient Escherichia coli CcI 21b cells | Caulobacter vibrioides |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.6.1.54 | EDTA | complete inhibition at 2 or 0.2 mM | Caulobacter vibrioides |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.6.1.54 | 0.105 | - |
UDP-2,3-diacylglucosamine | in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication | Caulobacter vibrioides |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.4.1.182 | mitochondrion | - |
Arabidopsis thaliana | 5739 | - |
2.4.1.182 | additional information | lipid X levels in mitochondria are 3 and 48fold higher than in chloroplasts or whole cell homogenates, respectively. Lipid X is undetectable in the plasma membrane | Arabidopsis thaliana | - |
- |
3.6.1.54 | membrane | - |
Caulobacter vibrioides | 16020 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.6.1.54 | Co2+ | the apparent specific activity of purified enzyme increases 6fold in the presence of added Co2+ | Caulobacter vibrioides | |
3.6.1.54 | Mg2+ | the apparent specific activity of purified enzyme increases 10fold in the presence of Mg2+ versus no added metal. Enzyme activity is maximal at 0.2 mM Mg2+ and remains approximately the same up to 20 mM Mg2+ | Caulobacter vibrioides | |
3.6.1.54 | Mn2+ | the apparent specific activity of purified enzyme increases 6fold in the presence of added Mn2+ | Caulobacter vibrioides |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.182 | additional information | Arabidopsis thaliana | formation of lipid A disaccharide from UDP-GlcNAc and lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, releasing UDP. Lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, bears two R-3-hydroxymyristoyl chains in Arabidopsis thaliana and is a key precursor of lipid A. No other lipid X molecular species are detected | ? | - |
? | |
2.4.1.182 | additional information | Arabidopsis thaliana Col-0 | formation of lipid A disaccharide from UDP-GlcNAc and lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, releasing UDP. Lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, bears two R-3-hydroxymyristoyl chains in Arabidopsis thaliana and is a key precursor of lipid A. No other lipid X molecular species are detected | ? | - |
? | |
2.4.1.182 | UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | Arabidopsis thaliana | - |
UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | - |
? | |
2.4.1.182 | UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | Arabidopsis thaliana Col-0 | - |
UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | - |
? |
EC Number | Organic Solvent | Comment | Organism |
---|---|---|---|
3.6.1.54 | Triton X-100 | while stimulated about 3fold in the presence of 0.05% (w/v) Triton X-100, the apparent activity does not decrease at high concentrations of Triton X-100 | Caulobacter vibrioides |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.182 | Arabidopsis thaliana | F4IF99 | - |
- |
2.4.1.182 | Arabidopsis thaliana Col-0 | F4IF99 | - |
- |
3.6.1.54 | Caulobacter vibrioides | A0A0H3C8Q1 | - |
- |
3.6.1.54 | Caulobacter vibrioides CB15 | A0A0H3C8Q1 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.6.1.54 | High-Trap Q Sepharose column chromatography and Superdex 200 gel filtration | Caulobacter vibrioides |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
3.6.1.54 | 25 | - |
membane-free lysate, in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication | Caulobacter vibrioides |
3.6.1.54 | 30 | - |
after 1.2fold purification, in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication | Caulobacter vibrioides |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.182 | additional information | formation of lipid A disaccharide from UDP-GlcNAc and lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, releasing UDP. Lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, bears two R-3-hydroxymyristoyl chains in Arabidopsis thaliana and is a key precursor of lipid A. No other lipid X molecular species are detected | Arabidopsis thaliana | ? | - |
? | |
2.4.1.182 | additional information | formation of lipid A disaccharide from UDP-GlcNAc and lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, releasing UDP. Lipid X, i.e. 2,3-diacylglucosamine 1-phosphate, bears two R-3-hydroxymyristoyl chains in Arabidopsis thaliana and is a key precursor of lipid A. No other lipid X molecular species are detected | Arabidopsis thaliana Col-0 | ? | - |
? | |
2.4.1.182 | UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | - |
Arabidopsis thaliana | UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | - |
? | |
2.4.1.182 | UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | - |
Arabidopsis thaliana Col-0 | UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(1->6)-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate | - |
? | |
3.6.1.54 | UDP-2,3-diacylglucosamine + H2O | the enzyme is selective for UDP-2,3-diacylglucosamine | Caulobacter vibrioides | 2,3-diacylglucosamine 1-phosphate + UMP | - |
? | |
3.6.1.54 | UDP-2,3-diacylglucosamine + H2O | the enzyme is selective for UDP-2,3-diacylglucosamine | Caulobacter vibrioides CB15 | 2,3-diacylglucosamine 1-phosphate + UMP | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.182 | LpxB | - |
Arabidopsis thaliana |
3.6.1.54 | LpxI | - |
Caulobacter vibrioides |
3.6.1.54 | UDP-2,3-diacylglucosamine pyrophosphatase | - |
Caulobacter vibrioides |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.6.1.54 | 7 | 9 | - |
Caulobacter vibrioides |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.1.182 | malfunction | 42fold accumulation of 2,3-diacylglucosamine 1-phosphate in Arabidopsis thaliana atlpxb-1 mutant | Arabidopsis thaliana |
3.6.1.54 | malfunction | UDP-2,3-diacylglucosamine-deficiency results in lethality | Caulobacter vibrioides |