Information on EC 2.4.1.70 - poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase

for references in articles please use BRENDA:EC2.4.1.70
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The expected taxonomic range for this enzyme is: Staphylococcus aureus

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EC NUMBER
COMMENTARY hide
2.4.1.70
-
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RECOMMENDED NAME
GeneOntology No.
poly(ribitol-phosphate) alpha-N-acetylglucosaminyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
n UDP-N-acetyl-alpha-D-glucosamine + 4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n UDP + 4-O-(2-N-acetyl-alpha-D-glucosaminyl-D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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-
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
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-
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:4-O-(D-ribitylphospho)n-di[(2R)-1-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol alpha-N-acetyl-D-glucosaminyltransferase (configuration-retaining)
Involved in the synthesis of teichoic acids.
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CAS REGISTRY NUMBER
COMMENTARY hide
37277-71-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains H or Duncan: primarily N-acetyl-beta-glucosamine transfer, strain 3528: N-acetyl-alpha-glucosamine transfer, strain Copenhagen: both transferases
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-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucose + poly(ribitol phosphate)
UDP + glucosyl-poly(ribitol phosphate)
show the reaction diagram
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10% of activity with UDP-N-acetyl-D-glucosamine
-
?
UDP-N-acetyl-D-glucosamine + poly(ribitol phosphate)
UDP + N-acetyl-D-glucosaminyl-poly(ribitol phosphate)
show the reaction diagram
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D-alanyl-N-acetyl-alpha-galactosamine poly(ribitol phosphate) is a less efficient acceptor, poor donor substrate is UDPglucose, no activity with teichoic acid, D-ribitol 5-phosphate or partial alkali hydrolysates of teichoic acid or N-acetyl-galactosamine polyribitol phosphate, UDP-N-acetyl-galactosamine, N-acetyl-galactosamine and N-acetyl-galactosamine phosphate
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ir
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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-D-glucosamine + poly(ribitol phosphate)
UDP + N-acetyl-D-glucosaminyl-poly(ribitol phosphate)
show the reaction diagram
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D-alanyl-N-acetyl-alpha-galactosamine poly(ribitol phosphate) is a less efficient acceptor, poor donor substrate is UDPglucose, no activity with teichoic acid, D-ribitol 5-phosphate or partial alkali hydrolysates of teichoic acid or N-acetyl-galactosamine polyribitol phosphate, UDP-N-acetyl-galactosamine, N-acetyl-galactosamine and N-acetyl-galactosamine phosphate
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ir
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
slight activation
Co2+
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slight activation
Mg2+
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8 mM, required for activity
Mn2+
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slight activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
poly(ribitol phosphate)
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-
0.7
UDP-N-acetylglucosamine
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen, N-acetyl-alpha-D-glucosamine transferase, not N-acetyl-beta-D-glucosamine transferase, a few months
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.70)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)