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Literature summary extracted from

  • Lehrer, J.; Vigeant, K.A.; Tatar, L.D.; Valvano, M.A.
    Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide (2007), J. Bacteriol., 189, 2618-2628.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.33
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.7.8.33 D156E no detectable transfer activity Escherichia coli
2.7.8.33 D156N no detectable transfer activity Escherichia coli
2.7.8.33 D159E transfer activity is drastically reduced, compared to wild-type enzyme Escherichia coli
2.7.8.33 D159N transfer activity is drastically reduced, compared to wild-type enzyme Escherichia coli
2.7.8.33 D90E slightly reduced velocities and small increases in the apparent Km for UDPGlcNAc. In membranes containing the D90E form of WecA, the apparent Km values for Mg2+ and Mn2+ increases 3-5fold compared to the apparent Km of the parental enzyme Escherichia coli
2.7.8.33 D90N slightly reduced velocities and small increases in the apparent Km for UDPGlcNAc. In membranes containing the D90N form of WecA, the apparent Km values for Mg2+ and Mn2+ increases 3-5fold compared to the apparent Km of the parental enzyme Escherichia coli
2.7.8.33 D91E membranes containing WecA-D91E exhibit a 6fold decrease in the apparent Km for UDP-GlcNAc compared to the apparent Km of the wild-type enzyme. In membranes containing the D91E form of WecA, the apparent Km values with Mg2+ decreases 3fold, compared to the apparent Km of the wild-type parental enzyme Escherichia coli
2.7.8.33 D91N in membranes containing the D91N form of WecA, the apparent Km values with Mg2+ increases 3fold, compared to the apparent Km of the wild-type parental enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.8.33 0.00012
-
 UDP-N-acetyl-D-glucosamine pH 8.5, 37°C, in presence of Mg2+ Escherichia coli
2.7.8.33 0.00019
-
 UDP-N-acetyl-D-glucosamine pH 8.5, 37°C, in presence of Mn2+ Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.8.33 membrane integral membrane protein. the C terminus of WecA is exposed to the cytosol. Localizes to discrete regions in the bacterial plasma membrane Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.33 Mg2+ either Mg2+ or Mn2+ activates the enzyme. In vitro and in the presence of excess UDP-GlcNAc, the enzyme is nearly six times more effective with Mn2+ than with Mg2+. KM-values for wild-type and mutant enzymes Escherichia coli
2.7.8.33 Mn2+ either Mg2+ or Mn2+ activates the enzyme. In vitro and in the presence of excess UDP-GlcNAc, the enzyme is nearly six times more effective with Mn2+ than with Mg2+. KM-values for wild-type and mutant enzymes Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.8.33 38000
-
 SDS-PAGE Escherichia coli
2.7.8.33 40957
-
 x * 40957, calculated from sequence Escherichia coli
2.7.8.33 40960
-
 calculated from sequence Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.33 UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate Escherichia coli initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.33 Escherichia coli P0AC78
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.8.33
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.33 UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide Escherichia coli UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
-
 ?
2.7.8.33 UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate Asp156 is required for catalysis Escherichia coli UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.8.33 ? x * 38000, SDS-PAGE Escherichia coli
2.7.8.33 ? x * 40957, calculated from sequence Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.8.33 WecA
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.8.33 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.8.33 8.5
-
 assay at Escherichia coli

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.8.33 Escherichia coli calculated from sequence
-
 10.01