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Literature summary for 2.7.8.33 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)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
D156E no detectable transfer activity Escherichia coli
D156N no detectable transfer activity Escherichia coli
D159E transfer activity is drastically reduced, compared to wild-type enzyme Escherichia coli
D159N transfer activity is drastically reduced, compared to wild-type enzyme Escherichia coli
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
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
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
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]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
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

Metals/Ions Comment Organism Structure
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
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]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Escherichia coli P0AC78
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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

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

Synonyms

Synonyms Comment Organism
WecA
-
Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

pI Value

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