Cloned (Comment) | Organism |
---|---|
gene wecA, cloning in Escherichia coli strain DH5alpha | Thermotoga maritima |
Protein Variants | Comment | Organism |
---|---|---|
D72A | site-directed mutagenesis, very low activity of the mutant protein at pH 8.0, which represents only about 1.2% of the wild-type activity. At pH 7.0, the mutant protein is totally inactive. Increasing the pH from 8 to 9 results in a 2.5fold increase of the D72A mutant activity, while the wild-type enzyme activity rather decreases, from 310 to 240 U/mg of protein | Thermotoga maritima |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
dodecylamine | - |
Thermotoga maritima |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell wall | - |
Thermotoga maritima | 5618 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | essentially required | Thermotoga maritima |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate | Thermotoga maritima | the enzyme is highly specific for UDP-GlcNAc, its physiological substrate | UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | - |
r | |
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate | Thermotoga maritima ATCC 43589 | the enzyme is highly specific for UDP-GlcNAc, its physiological substrate | UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermotoga maritima | Q9X1N5 | gene wecA | - |
Thermotoga maritima ATCC 43589 | Q9X1N5 | gene wecA | - |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and D72A mutant enzymes | Thermotoga maritima |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | a one-step, single displacement mechanism. The oxyanion of the polyprenyl-phosphate attacks the beta-phosphate of the nucleotide substrate, leading to the formation of lipid product and the liberation of UMP. The involvement of an invariant aspartyl residue in the deprotonation of the lipid substrate is possible | Thermotoga maritima |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme does not display any diphosphatase activity on the nucleotide substrate. Enzyme catalytic mechanism and substrate specificity, overview. The minimal length of the carbon chain of the lipid substrate for an efficient catalysis is 35. The essential aspartate residue, that is invariant in the superfamily, is Asp72 in Thermotoga maritima WecA, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. No activity by the enzyme with UDP-galactose, UDP-GalNAc, GDP-glucose, ADP-ribose, UDP-glucuronic acid, GDP-D-mannose, and UDP-hexanolamine | Thermotoga maritima | ? | - |
? | |
additional information | the enzyme does not display any diphosphatase activity on the nucleotide substrate. Enzyme catalytic mechanism and substrate specificity, overview. The minimal length of the carbon chain of the lipid substrate for an efficient catalysis is 35. The essential aspartate residue, that is invariant in the superfamily, is Asp72 in Thermotoga maritima WecA, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. No activity by the enzyme with UDP-galactose, UDP-GalNAc, GDP-glucose, ADP-ribose, UDP-glucuronic acid, GDP-D-mannose, and UDP-hexanolamine | Thermotoga maritima ATCC 43589 | ? | - |
? | |
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate | the enzyme is highly specific for UDP-GlcNAc, its physiological substrate | Thermotoga maritima | UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | - |
r | |
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate | the forward and reverse exchange reactions required the presence of the second substrate, undecaprenyl phosphate and UMP, respectively. The nucleotide substrate UDPMurNAc-pentapeptide, as well as the nucleotide product UMP, can bind to MraY in the absence of lipid ligands. The enzyme is highly specific for UDP-GlcNAc, its physiological substrate | Thermotoga maritima | UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | - |
r | |
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate | the enzyme is highly specific for UDP-GlcNAc, its physiological substrate | Thermotoga maritima ATCC 43589 | UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | - |
r | |
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate | the forward and reverse exchange reactions required the presence of the second substrate, undecaprenyl phosphate and UMP, respectively. The nucleotide substrate UDPMurNAc-pentapeptide, as well as the nucleotide product UMP, can bind to MraY in the absence of lipid ligands. The enzyme is highly specific for UDP-GlcNAc, its physiological substrate | Thermotoga maritima ATCC 43589 | UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol | - |
r |
Synonyms | Comment | Organism |
---|---|---|
WecA | - |
Thermotoga maritima |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
assay at | Thermotoga maritima |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Thermotoga maritima |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase, P2HPT, superfamily | Thermotoga maritima |
metabolism | WecA catalyzes the first membrane step of the biosynthesis of many cell wall polymers such as the O-antigen, teichoic acids and arabinogalactan | Thermotoga maritima |
physiological function | enzyme WecA, catalyzes the transfer of the phospho-GlcNAc moiety of UDP-N-acetylglucosamine onto the same lipid carrier, leading to the formation of N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol that is essential for the synthesis of various bacterial cell envelope components. Undecaprenyl diphosphoryl-N-acetylglucosamine (lipid intermediate I) is a ubiquitous compound in all kingdoms of life. the enzyme is involved in the initiation of enterobacterial common antigen biosynthesis | Thermotoga maritima |