Information on EC 2.7.8.33 - UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.33
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate = UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
beta-D-galactosaminyl-(1rarr;3)-N-acetyl-alpha-D-galactosamine biosynthesis
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-
enterobacterial common antigen biosynthesis
-
-
Escherichia coli serotype O86 O-antigen biosynthesis
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poly(3-O-beta-D-glucopyranosyl-N-acetylgalactosamine 1-phosphate) wall teichoic acid biosynthesis
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poly(glycerol phosphate) wall teichoic acid biosynthesis
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poly(ribitol phosphate) wall teichoic acid biosynthesis I (B. subtilis)
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poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
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-
teichoic acid 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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
TagO; gene tagO
UniProt
Manually annotated by BRENDA team
TagO; gene tagO
UniProt
Manually annotated by BRENDA team
gene wecA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
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-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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 + dodecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-dodecaprenol
show the reaction diagram
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
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 + octaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-octaprenol
show the reaction diagram
as active as ditrans,polycis-undecaprenyl phosphate. A minimal length of 35 carbons is required for the lipid substrate
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-
?
UDP-N-acetyl-D-glucosamine + pentadecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-pentadecaprenol
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
UDP-N-acetyl-D-glucosamine + ditrans,polycis-undecaprenyl phosphate
UMP + N-acetyl-D-glucosaminyldiphospho-ditrans,polycis-undecaprenol
show the reaction diagram
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
caprazamycin B
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CHAPS
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i.e 3-[(3-cholamidopropyl)-dimethylammonio]-lpropane-sulfonate
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
KCl
125 mM, about 50% of maximal activity
Mg2+
250 mM, no activity. 10 mM Mg2+ optimally activates the enzyme
NaCl
200 mM, about 50% of maximal activity
tunicamycin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,6,9,12,15,18-hexaoxatriacontan-1-ol
i.e. C12E6, optimal concentration is 90-200 mM
Triton X-100
optimal concentration is 50-120 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
ditrans,polycis-undecaprenyl phosphate
pH 8, 65°C
0.00007 - 0.62
UDP-N-acetyl-D-glucosamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
ditrans,polycis-undecaprenyl phosphate
Thermotoga maritima
Q9X1N5
pH 8, 65°C
1.2
UDP-N-acetyl-D-glucosamine
Thermotoga maritima
Q9X1N5
pH 8, 65°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015
caprazamycin B
Bacillus subtilis
O34753
pH and temperature not specified in the publication
0.00005
CPZEN-45
Bacillus subtilis
O34753
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.2895
pH 8, 65°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
pH 6.5: about 50% of maximal activity, pH 9.5: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 67
50°C: about 50% of maximal activity, 67°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.01
-
calculated from sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33876
x * 33876, calculated from sequence
33880
calculated from sequence
38000
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SDS-PAGE
40957
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x * 40957, calculated from sequence
40960
-
calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Co2+ affinity chromatography
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n-dodecyl-beta-D-maltoside is the most efficient detergent for both the extraction and purification steps of the WecA protein
recombinant wild-type and D72A mutant enzymes
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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expressed in Escherichia coli MV501 cells
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gene wecA, cloning in Escherichia coli strain DH5alpha
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D156E
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no detectable transfer activity
D156N
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no detectable transfer activity
D159E
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transfer activity is drastically reduced, compared to wild-type enzyme
D159N
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transfer activity is drastically reduced, compared to wild-type enzyme
D217A
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the mutation results in reduced enzymatic activity
D217E
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the mutation results in a slightly more active enzyme
D217K
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inactive
D217N
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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
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the mutation results in a more active enzyme
D90E
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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
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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
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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
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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
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the mutation results in severely reduced enzymatic activity
G216A
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inactive
M215A
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the mutation results in a slightly more active enzyme
V213A
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the mutation results in severely reduced enzymatic activity
Show AA Sequence (1745 entries)
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