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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
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
-
-
?
UDP-N-acetyl-D-glucosamine + octaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-octaprenol
as active as ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
additional information
?
-
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
the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
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
-
-
r
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
Asp156 is required for catalysis
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
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
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
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
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
the product ditrans,polycis-undecaprenyl-N-acetyl-D-glucosaminyl diphosphate is an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
a minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
the reverse reaction is about 1% of the forward reaction
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
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
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
a minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + dodecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-dodecaprenol
about 85% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + dodecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-dodecaprenol
about 85% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
-
-
-
?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
about 80% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
about 80% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
-
-
?
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
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
-
-
?
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
about 70% of the activity compared to ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
-
-
?
additional information
?
-
-
wecAHP complementes O antigen synthesis in the Escherichia coli wecA mutant
-
-
?
additional information
?
-
no activity with farnesyl phosphate and geranylgeranyl phosphate. Heptaprenyl phosphate shows 3% of the activity compared to ditrans,polycis-undecaprenyl phosphate
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
no activity with farnesyl phosphate and geranylgeranyl phosphate. Heptaprenyl phosphate shows 3% of the activity compared to ditrans,polycis-undecaprenyl phosphate
-
-
?
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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
-
-
-
?
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
the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
the enzyme is highly specific for UDP-GlcNAc, its physiological substrate
-
-
r
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
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
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
the product ditrans,polycis-undecaprenyl-N-acetyl-D-glucosaminyl diphosphate is an essential lipid intermediate for the biosynthesis of various bacterial cell envelope components
-
-
?
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
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
-
-
?
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D156E
no detectable transfer activity
D156N
no detectable transfer activity
D159E
transfer activity is drastically reduced, compared to wild-type enzyme
D159N
transfer activity is drastically reduced, compared to wild-type enzyme
D217A
-
the mutation results in reduced enzymatic activity
D217E
-
the mutation results in a slightly more active 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
D217S
-
the mutation results in a more active enzyme
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
F214A
-
the mutation results in severely reduced enzymatic activity
M215A
-
the mutation results in a slightly more active enzyme
V213A
-
the mutation results in severely reduced enzymatic activity
T728G
naturally occuring mutation in TagO leading to CPZEN-45 resistance
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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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