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Information on EC 2.7.8.33 - UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase and Organism(s) Escherichia coli and UniProt Accession P0AC78

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IUBMB Comments
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 and of teichoic acid in certain Gram-positive bacteria .
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This record set is specific for:
Escherichia coli
UNIPROT: P0AC78
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
weca transferase, glcnac-p-p-und synthase, undecaprenyl-phosphate-glcnac-1-phosphate transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GlcNAc-P-P-Und synthase
-
GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
-
UDP-GlcNAc:undecaprenyl phosphate N-acetylglucosaminyl 1-P transferase
-
UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase
-
polyisoprenyl-phosphate N-acetylaminosugar-1-phosphate transferase
-
-
polyprenyl-P N-acetylhexosamine-1-P transferase
-
-
undecaprenyl-phosphate N-acetylhexosamine-1-phosphate transferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
show the reaction diagram
UDP-N-acetyl-D-glucosamine + nonaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-nonaprenol
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + heptaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-heptaprenol
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
show the reaction diagram
initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
i.e 3-[(3-cholamidopropyl)-dimethylammonio]-lpropane-sulfonate
tunicamycin
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00012 - 0.0056
UDP-N-acetyl-D-glucosamine
0.00007 - 0.00008
UDP-N-acetyl-D-glucosamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.01
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
SDS-PAGE
40957
x * 40957, calculated from sequence
40960
calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
D217A
-
the mutation results in reduced enzymatic activity
D217E
-
the mutation results in a slightly more active enzyme
D217K
-
inactive
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
F214A
-
the mutation results in severely reduced enzymatic activity
G216A
-
inactive
M215A
-
the mutation results in a slightly more active enzyme
V213A
-
the mutation results in severely reduced enzymatic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Co2+ affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expressed in Escherichia coli MV501 cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Hug, I.; Feldman, M.F.
Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria
Glycobiology
21
138-151
2011
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team