Information on EC 2.4.1.58 - lipopolysaccharide glucosyltransferase I

Word Map on EC 2.4.1.58
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:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.58
-
RECOMMENDED NAME
GeneOntology No.
lipopolysaccharide glucosyltransferase I
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + lipopolysaccharide = UDP + D-glucosyl-lipopolysaccharide
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Lipid A-core biosynthesis
-
-
Lipopolysaccharide biosynthesis
-
-
Metabolic pathways
-
-
lipid A biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:lipopolysaccharide glucosyltransferase
Transfers glucosyl residues to the backbone portion of lipopolysaccharide [cf. EC 2.4.1.44 (lipopolysaccharide 3-alpha-galactosyltransferase, EC 2.4.1.56 (lipopolysaccharide N-acetylglucosaminyltransferase) and EC 2.4.1.73 (lipopolysaccharide glucosyltransferase II)].
CAS REGISTRY NUMBER
COMMENTARY hide
9074-00-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K12 CS520, recombinant enzyme expressed in Salmonella typhimurium
-
-
Manually annotated by BRENDA team
strain K12 CS520, recombinant enzyme expressed in Salmonella typhimurium
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UDPglucose + lipopolysaccharide
UDP + D-glucosyllipopolysaccharide
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
UDPglucose + lipopolysaccharide
UDP + D-glucosyllipopolysaccharide
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
requires divalent cation, in decreasing order of effectiveness: Mg2+, Ba2+, Ca2+, Co2+, relative activities: Mg2+: 1.0, Ba2+: 0.77, Ca2+: 0.65, Co2+: 0.31
Ca2+
-
requires divalent cation, in decreasing order of effectiveness: Mg2+, Ba2+, Ca2+, Co2+, relative activities: Mg2+: 1.0, Ba2+: 0.77, Ca2+: 0.65, Co2+: 0.31
Co2+
-
requires divalent cation, in decreasing order of effectiveness: Mg2+, Ba2+, Ca2+, Co2+, relative activities: Mg2+: 1.0, Ba2+: 0.77, Ca2+: 0.65, Co2+: 0.31
Mn2+
-
soluble enzyme: MgCl2 stimulates more than MnCl2
additional information
-
requires divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
not inhibited by p-chloromercuribenzoate, no detectable inhibition by non-substrate lipopolysaccharides obtained from other mutant strains of Salmonella typhimurium: G30G, G30A, G30, TV119, LT2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphatidylethanolamine
-
requirement, most effective phospholipid, phosphatidylethanolamine containing unsaturated or cyclopropane acyl groups is more effective than that containing saturated acyl groups
Phospholipid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.1
lipopolysaccharide
0.074 - 0.33
UDPglucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
Tris-maleate or Tris-Cl buffers
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
several peaks suggesting aggregation of enzyme, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing: rapid loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C or 4°C, soluble enzyme, overnight storage, 30-50% loss of activity
-
4°C, 20% glycerol, for about 5 days: retains full activity, 10% loss of activity per week thereafter
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of a suicide vector
-
expressed in Haemophilus influenzae delta-lic2B
-
expression in Neisseria meningitidis; expression in Neisseria meningitidis; expression in Neisseria meningitidis
rfaG gene encodes enzyme, use of hybrid ColE1 plasmids containing Escherichia coli genes for glycosyltransferases to introduce enzyme into Salmonella typhimurium strains SL1032/pL10-7 and pLC17-24 lacking enzyme, plasmids are capable of correcting the transferase defect
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (376 entries)
Please use the Sequence Search for a specific query.