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Literature summary for 2.7.8.33 extracted from

  • Al-Dabbagh, B.; Olatunji, S.; Crouvoisier, M.; El Ghachi, M.; Blanot, D.; Mengin-Lecreulx, D.; Bouhss, A.
    Catalytic mechanism of MraY and WecA, two paralogues of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily (2016), Biochimie, 127, 249-257.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene wecA, cloning in Escherichia coli strain DH5alpha Thermotoga maritima

Protein Variants

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

Inhibitors Comment Organism Structure
dodecylamine
-
Thermotoga maritima

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
Thermotoga maritima 5618
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ essentially required Thermotoga maritima

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Thermotoga maritima Q9X1N5 gene wecA
-
Thermotoga maritima ATCC 43589 Q9X1N5 gene wecA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and D72A mutant enzymes Thermotoga maritima

Reaction

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 and Products (Substrate)

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

Synonyms Comment Organism
WecA
-
Thermotoga maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
assay at Thermotoga maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Thermotoga maritima

General Information

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