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Information on EC 2.7.8.33 - UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
for references in articles please use BRENDA:EC2.7.8.33
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.8 Transferases for other substituted phosphate groups
2.7.8.33 UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
IUBMB Comments
This enzyme catalyses the synthesis of N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 and of teichoic acid in certain Gram-positive bacteria .
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
showSynonyms
weca transferase, glcnac-p-p-und synthase, undecaprenyl-phosphate-glcnac-1-phosphate transferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
TagO
UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase
-
UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
-
undecaprenyl-phosphate-GlcNAc-1-phosphate transferase
WecA
UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
-
UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
-
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
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
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
enterobacterial common antigen biosynthesis, Escherichia coli serotype O:104 O antigen biosynthesis, Escherichia coli serotype O:107 O antigen biosynthesis, Escherichia coli serotype O:111/Salmonella enterica serotype O:35 O antigen biosynthesis, Escherichia coli serotype O:117 O antigen biosynthesis, Escherichia coli serotype O:127 O antigen biosynthesis, Escherichia coli serotype O:128 O antigen biosynthesis, Escherichia coli serotype O:149/Shigella boydii serotype O1 O antigen biosynthesis, Escherichia coli serotype O:15 O antigen biosynthesis, Escherichia coli serotype O:152 O antigen biosynthesis, Escherichia coli serotype O:157/Salmonella enterica serotype O:30 O antigen biosynthesis, Escherichia coli serotype O:169 O antigen biosynthesis, Escherichia coli serotype O:177 O antigen biosynthesis, Escherichia coli serotype O:183/Shigella boydii serotype O:10 O antigen biosynthesis, Escherichia coli serotype O:1B/Salmonella enterica serotype O:42 O antigen biosynthesis, Escherichia coli serotype O:2 O antigen biosynthesis, Escherichia coli serotype O:21/Salmonella enterica serotype O:38 O antigen biosynthesis, Escherichia coli serotype O:49 O antigen biosynthesis, Escherichia coli serotype O:50 O antigen biosynthesis, Escherichia coli serotype O:51/Salmonella enterica serotype O:57 O antigen biosynthesis, Escherichia coli serotype O:52 O antigen biosynthesis, Escherichia coli serotype O:55/Salmonella enterica serotype O:50 O antigen biosynthesis, Escherichia coli serotype O:56 O antigen biosynthesis, Escherichia coli serotype O:7 O antigen biosynthesis, Escherichia coli serotype O:71/Salmonella enterica serotype O:28ac O antigen biosynthesis, Escherichia coli serotype O:77/Salmonella enterica serotype O:6,14 O antigen biosynthesis, Escherichia coli serotype O:8 O antigen biosynthesis, Escherichia coli serotype O:85/Salmonella enterica serotype O:17 O antigen biosynthesis, Escherichia coli serotype O:86 O antigen biosynthesis, Escherichia coli serotype O:9 O antigen biosynthesis, Escherichia coli serotype O:9a O antigen biosynthesis, H. pylori 26695 O-antigen biosynthesis, poly(3-O-beta-D-glucopyranosyl-N-acetylgalactosamine 1-phosphate) wall teichoic acid biosynthesis, poly(glycerol phosphate) wall teichoic acid biosynthesis, poly(ribitol phosphate) wall teichoic acid biosynthesis I (B. subtilis), poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus), Salmonella enterica serotype O:13 O antigen biosynthesis, Salmonella enterica serotype O:18 O antigen biosynthesis, Salmonella enterica serotype O:39 O antigen biosynthesis, Salmonella enterica serotype O:54 O antigen biosynthesis, Salmonella enterica serotype O:6,7 O antigen biosynthesis, Shigella boydii serotype 6 O antigen biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-D-glucosaminephosphotransferase
This enzyme catalyses the synthesis of N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components. The enzyme also initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide in certain Escherichia coli strains, including K-12 [2] and of teichoic acid in certain Gram-positive bacteria [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
UDP-N-acetyl-D-glucosamine + dodecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-dodecaprenol
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
UDP-N-acetyl-D-glucosamine + nonaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-nonaprenol
Substrates: the enzyme has a strict preference for fully unsaturated polyprenyl phosphate substrates. Undecaprenyl phosphate and pentadecaprenyl phosphate are utilized with higher catalytic efficiency compared to nonaprenyl phosphate
Products: -
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?
UDP-N-acetyl-D-glucosamine + octaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-octaprenol
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: -
Products: -
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UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
Products: -
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r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: 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
Products: -
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r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
Products: -
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r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: 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
Products: -
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r
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: Asp156 is required for catalysis
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: the enzyme has a strict preference for fully unsaturated polyprenyl phosphate substrates. Undecaprenyl phosphate and pentadecaprenyl phosphate are utilized with higher catalytic efficiency compared to nonaprenyl phosphate
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
-
Substrates: -
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: the enzyme catalyzes the first membrane step of the biosynthesis of various polymers of the bacterial cell wall such as the O-antigen and enterobacterial common antigen
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: the product ditrans,polycis-undecaprenyl-N-acetyl-D-glucosaminyl diphosphate is an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: a minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: the reverse reaction is about 1% of the forward reaction
Products: -
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?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: the enzyme catalyzes the first membrane step of the biosynthesis of various polymers of the bacterial cell wall such as the O-antigen and enterobacterial common antigen
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: a minimal length of 35 carbons is required for the lipid substrate
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + dodecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-dodecaprenol
Substrates: about 85% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + dodecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-dodecaprenol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: about 85% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
-
Substrates: -
Products: -
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?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
Substrates: about 80% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: about 80% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + octaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-octaprenol
Substrates: as active as ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + octaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-octaprenol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: as active as ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
Substrates: the enzyme has a strict preference for fully unsaturated polyprenyl phosphate substrates. Undecaprenyl phosphate and pentadecaprenyl phosphate are utilized with higher catalytic efficiency compared to nonaprenyl phosphate
Products: -
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?
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
Substrates: about 70% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
Products: -
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?
additional information
?
-
-
Substrates: wecAHP complementes O antigen synthesis in the Escherichia coli wecA mutant
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additional information
?
-
Substrates: no activity with farnesyl phosphate and geranylgeranyl phosphate. Heptaprenyl phosphate shows 3% of the activity compared to ditrans,polycis-undecaprenyl phosphate
Products: -
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?
additional information
?
-
Substrates: 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
Products: -
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?
additional information
?
-
Substrates: 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
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
Products: -
Products: -
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Substrates: the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
Products: -
Products: -
r
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: the enzyme catalyzes the first membrane step of the biosynthesis of various polymers of the bacterial cell wall such as the O-antigen and enterobacterial common antigen
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Substrates: the product ditrans,polycis-undecaprenyl-N-acetyl-D-glucosaminyl diphosphate is an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components
Products: -
Products: -
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Substrates: the enzyme catalyzes the first membrane step of the biosynthesis of various polymers of the bacterial cell wall such as the O-antigen and enterobacterial common antigen
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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
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
Mg2+
absolute requirement for a divalent cation (Mg2+), optimal activity at 10 mM, inhibitory at higher conventrations, no activity in absence of Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CPZEN-45
the primary target of CPZEN-45 in Bacillus subtilis is TagO, which is a different target from that of the parent caprazamycins. CPZEN-45 is not effective against a strain overexpressing undecaprenyl-phosphate-GlcNAc-1-phosphate transferase (TagO, involved in the biosynthesis of teichoic acid) due to a mutation T728G in the tagO gene ir responsible for the spontaneous CPZEN-45-resistant strain. Very poor inhibition by vancomycin
Mg2+
250 mM, no activity. 10 mM Mg2+ optimally activates the enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,6,9,12,15,18-hexaoxatriacontan-1-ol
i.e. C12E6, optimal concentration is 90-200 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00007
UDP-N-acetyl-D-glucosamine
-
mutant enzyme, in 50 mM of Tris-HCl (pH 8.0), 40 mM of MgCl2, at 37°C
0.00008
UDP-N-acetyl-D-glucosamine
-
wild type enzyme, in 50 mM of Tris-HCl (pH 8.0), 40 mM of MgCl2, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00015
caprazamycin B
Bacillus subtilis
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
pH 6.5: about 50% of maximal activity, pH 9.5: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 67
50°C: about 50% of maximal activity, 67°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
integral membrane protein. the C terminus of WecA is exposed to the cytosol. Localizes to discrete regions in the bacterial plasma membrane
brenda
modelling of the topology of WecA taking into account the available experimental data from the topological analysis of MraY
brenda
design of a vector system to generate C-terminal protein fusions to the FLAG epitope, which is used to find conditions to monitor WecA by immunoblot analysis with anti-FLAG antibodies, to determine the correct site for initiation of translation, and to investigate the localization of hybrid proteins in the cytoplasmic membrane
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
the enzyme is a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase, P2HPT, superfamily
evolution
-
the enzyme is a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase, P2HPT, superfamily
-
metabolism
WecA catalyzes the first membrane step of the biosynthesis of many cell wall polymers such as the O-antigen, teichoic acids and arabinogalactan
metabolism
the enzyme is involved in the biosynthetic pathway of peptidoglycan and teichoic acid in Bacillus subtilis strain 168, overview
metabolism
-
the enzyme is involved in the biosynthetic pathway of peptidoglycan and teichoic acid in Bacillus subtilis strain 168, overview
-
metabolism
-
WecA catalyzes the first membrane step of the biosynthesis of many cell wall polymers such as the O-antigen, teichoic acids and arabinogalactan
-
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
physiological function
strains lacking transcription regulator component CpxAR or WecA are more susceptible to these stresses than the wild-type, but the complemented strains show phenotypes similar to those of the wild-type. Mice infected with strains lacking CpxAR or WecA activity exhibit lower mortality and bacterial loads in the lung than those infected with the wild-type or complemented strains
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
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Show AA Sequence and Transmembrane Helices (1809 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T728G
D159E
transfer activity is drastically reduced, compared to wild-type enzyme
D159N
transfer activity is drastically reduced, compared to wild-type enzyme
D217N
-
the mutation results in a more active enzyme and leads to more than 2fold increase in Vmax without significant change in the Km for the UDP-N-acetyl-D-glucosamine
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
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
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
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
D72A
T728G
naturally occuring mutation in TagO leading to CPZEN-45 resistance
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
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
n-dodecyl-beta-D-maltoside is the most efficient detergent for both the extraction and purification steps of the WecA protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into pET2130, generating the plasmid pWTM8. The wecA gene product is expressed with an N-terminal polyhistidine tag, expression in Escherichia coli C43(DE3)
design of a vector system to generate C-terminal protein fusions to the FLAG epitope, which is used to find conditions to monitor WecA by immunoblot analysis with anti-FLAG antibodies, to determine the correct site for initiation of translation, and to investigate the localization of hybrid proteins in the cytoplasmic membrane
detailed examination of the role of a conserved motif within the predicted large cytosolic loop
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CpxR positively regulates WecA expression by directly binding to the putative promoter region of WecA
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Al-Dabbagh, B.; Blanot, D.; Mengin-Lecreulx, D.; Bouhss, A.
Preparative enzymatic synthesis of polyprenyl-pyrophosphoryl-N-acetylglucosamine, an essential lipid intermediate for the biosynthesis of various bacterial cell envelope polymers
Anal. Biochem.
391
163-165
2009
Thermotoga maritima (Q9X1N5)
brenda
Rush, J.S.; Rick, P.D.; Waechter, C.J.
Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase from E.coli
Glycobiology
7
315-322
1997
Escherichia coli (P0AC78)
brenda
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
J. Bacteriol.
189
2618-2628
2007
Escherichia coli (P0AC78)
brenda
Al-Dabbagh, B.; Mengin-Lecreulx, D.; Bouhss, A.
Purification and characterization of the bacterial UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase WecA
J. Bacteriol.
190
7141-7146
2008
Thermotoga maritima (Q9X1N5), Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 (Q9X1N5)
brenda
Amer, A.O.; Valvano, M.A.
Conserved amino acid residues found in a predicted cytosolic domain of the lipopolysaccharide biosynthetic protein WecA are implicated in the recognition of UDP-N-acetylglucosamine
Microbiology
147
3015-3025
2001
Escherichia coli (P0AC78)
brenda
Hug, I.; Couturier, M.R.; Rooker, M.M.; Taylor, D.E.; Stein, M.; Feldman, M.F.
Helicobacter pylori lipopolysaccharide is synthesized via a novel pathway with an evolutionary connection to protein N-glycosylation
PLoS Pathog.
6
e1000819
2010
Helicobacter pylori
brenda
Hug, I.; Feldman, M.F.
Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria
Glycobiology
21
138-151
2011
Escherichia coli
brenda
Furlong, S.E.; Valvano, M.A.
Characterization of the highly conserved VFMGD motif in a bacterial polyisoprenyl-phosphate N-acetylaminosugar-1-phosphate transferase
Protein Sci.
21
1366-1375
2012
Escherichia coli
brenda
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
Biochimie
127
249-257
2016
Thermotoga maritima (Q9X1N5), Thermotoga maritima ATCC 43589 (Q9X1N5)
brenda
Ishizaki, Y.; Hayashi, C.; Inoue, K.; Igarashi, M.; Takahashi, Y.; Pujari, V.; Crick, D.C.; Brennan, P.J.; Nomoto, A.
Inhibition of the first step in synthesis of the mycobacterial cell wall core, catalyzed by the GlcNAc-1-phosphate transferase WecA, by the novel caprazamycin derivative CPZEN-45
J. Biol. Chem.
288
30309-30319
2013
Bacillus subtilis (O34753), Bacillus subtilis, Bacillus subtilis 168 (O34753)
brenda
Yan, K.; Liu, T.; Duan, B.; Liu, F.; Cao, M.; Peng, W.; Dai, Q.; Chen, H.; Yuan, F.; Bei, W.
The CpxAR two-component system contributes to growth, stress resistance, and virulence of Actinobacillus pleuropneumoniae by upregulating wecA transcription
Front. Microbiol.
11
1026
2020
Actinobacillus pleuropneumoniae serotype 5b L20 (A3N2K2)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.8.33)
Transporter Classification Database (TCDB): 9.B.146.1.7
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