Information on EC 2.4.1.180 - lipopolysaccharide N-acetylmannosaminouronosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.180
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RECOMMENDED NAME
GeneOntology No.
lipopolysaccharide N-acetylmannosaminouronosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-mannosaminouronate + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = UDP + N-acetyl-beta-D-mannosaminouronyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
enterobacterial common antigen biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-beta-D-mannosaminouronate:lipid I N-acetyl-beta-D-mannosaminouronosyltransferase
Involved in the biosynthesis of common antigen in Enterobacteriaceae.
CAS REGISTRY NUMBER
COMMENTARY hide
113478-30-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
F1467, lacking enzyme activity and 21259, wild-type
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the 440 kDa enzyme complex, named teichuronic acid synthetase, TUAS, is an octomer composed of two kinds of glycosyltransferases, glucosyltransferase, and ManNAcA-transferase, which is capable of catalyzing the transfer of disaccharide glycosyl residues containing both glucose and the N-acetylmannosaminuronic acid residues. TUAS is a bifunctional glycosyltransferase capable of transferring both the component sugars, glucose and ManNAcA, for the TUA polymer. The purified TUAS contains carotinoids and lipids. TUAS serves as a multitasking polysaccharide assembling station on the bacterial membrane
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-mannosaminuronate + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP + N-acetyl-beta-D-mannosaminuronyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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?
UDP-N-acetyl-D-mannosaminuronic acid + N-acetyl-D-glucosamine-diphosphorylundecaprenol + 2 H+
UDP + ManNAcA-GlcNAc-diphosphorylundecaprenol + H2O
show the reaction diagram
additional information
?
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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-mannosaminuronic acid + N-acetyl-D-glucosamine-diphosphorylundecaprenol + 2 H+
UDP + ManNAcA-GlcNAc-diphosphorylundecaprenol + H2O
show the reaction diagram
additional information
?
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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TUAS embedded in the cell wall, pH 8.2, 25°C
8.7
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TUAS embedded in the vesicle membrane, pH 8.2, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
440000
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TUAS complex
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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4 * 54000 + 4 * 52500, TUAS complex, SDS-PAGE
additional information
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when the eight subunits disassociate, the protein loses its conformation as well as the catalytic function for TUA biosynthesis
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native TUAS complex partially by fractionation of Thesit-solubilized membrane fraction with ammonium sulfate
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
transfection of wild-type enzyme code to mutant
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Show AA Sequence (823 entries)
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