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

for references in articles please use BRENDA:EC2.4.1.70
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Staphylococcus aureus

top print hide
EC NUMBER
COMMENTARY hide
2.4.1.70
-
top print hide
RECOMMENDED NAME
GeneOntology No.
poly(ribitol-phosphate) N-acetylglucosaminyltransferase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + poly(ribitol phosphate) = UDP + (N-acetyl-alpha-D-glucosaminyl)poly(ribitol phosphate)
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:poly(ribitol-phosphate) N-acetyl-D-glucosaminyltransferase
Involved in the synthesis of teichoic acids.
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
37277-71-7
-
top print hide
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
-
-
Manually annotated by BRENDA team
top print hide
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
-
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
-
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
-
ir
top print hide
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
-
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
-
ir
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
slight activation
Co2+
-
slight activation
Mg2+
-
8 mM, required for activity
Mn2+
-
slight activation
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
poly(ribitol phosphate)
-
-
0.7
UDP-N-acetylglucosamine
-
-
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
frozen, N-acetyl-alpha-D-glucosamine transferase, not N-acetyl-beta-D-glucosamine transferase, a few months
-
top
top
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)