D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.1.264 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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D-Man-alpha-(1->3) -D-Glc-beta-(1->4) -D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase (EC 2.4.1.264, GumK) is an enzyme with the systematic name UDP-glucuronate: D-Man-alpha-(1->3) -D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol beta-1,2-glucuronyltransferase. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction:
The enzyme is involved in the biosynthesis of the exopolysaccharides xanthan (in the bacterium Xanthomonas campestris ) and acetan (in the bacterium Gluconacetobacter xylinus ).
Xanthan gum is a polysaccharide with many industrial uses, including as a common food additive. It is an effective thickening agent and stabilizer that prevents ingredients from separating. It can be produced from simple sugars by fermentation and derives its name from the species of bacteria used, Xanthomonas campestris.
Xanthomonas campestris is a gram-negative, obligate aerobic bacterium that is a member of the Xanthomonas genus, which is a group of bacteria that are commonly known for their association with plant disease. This species includes Xanthomonas campestris pv. campestris the cause of black rot of brassicas, one of the most important diseases of brasicas worldwide.
Xanthomonas is a genus of bacteria, many of which cause plant diseases. There are at least 27 plant associated Xanthomonas spp., that all together infect at least 400 plant species. Different species typically have specific host and/or tissue range and colonization strategies.
The enzyme xanthan lyase catalyzes the following process:
In enzymology, a galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction
GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase is an enzyme with systematic name GDP-mannose:GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4-beta-mannosyltransferase. This enzyme catalyses the following chemical reaction
GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase is an enzyme with systematic name GDP-mannose:D-Glc-beta-(1->4)-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 3-alpha-mannosyltransferase . This enzyme catalyses the following chemical reaction
Cyanidin-3-O-glucoside 2-O-glucuronosyltransferase is an enzyme with systematic name UDP-D-glucuronate:cyanidin-3-O-beta-D-glucoside 2-O-beta-D-glucuronosyltransferase. This enzyme catalyses the following chemical reaction
Soyasapogenol glucuronosyltransferase is an enzyme with systematic name UDP-D-glucuronate:soyasapogenol 3-O-D-glucuronosyltransferase. This enzyme catalyses the following chemical reaction
Rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,3/1,4-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 3-beta/4-beta-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction
Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase is an enzyme with systematic name UDP-alpha-D-galactofuranose:beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol 4-beta/5-beta-D-galactofuranosyltransferase. This enzyme catalyses the following chemical reaction
GalNAc5-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase is an enzyme with systematic name UDP-alpha-D-glucose:(GalNAc-alpha- )4-GalNAc-alpha-(1->3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol 3-beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction
Xanthan ketal pyruvate transferase is an enzyme with systematic name phosphoenolpyruvate:D-Man-beta-(1->4)-GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphospho-ditrans,octacis-undecaprenol 4,6-O-(1-carboxyethan-1,1-diyl)transferase. This enzyme catalyses the following chemical reaction
Undecaprenyl-phosphate glucose phosphotransferase is an enzyme with systematic name UDP-glucose:ditrans,octacis-undecaprenyl-phosphate glucose phosphotransferase. This enzyme catalyses the following chemical reaction
UDP-N-acetylglucosamine—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-alpha-D-glucosaminephosphotransferase. This enzyme catalyses the following chemical reaction
UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase. This enzyme catalyses the following chemical reaction
Methyltransferase/kinase WbdD EC 2.1.1.294 and EC 2.7.1.181WbdD is a bifunctional enzyme that regulates the length of the LPS O-antigen polysaccharide chain. Stops the polymerization of the chain by phosphorylating and then methylating the phosphate on the terminal sugar. This terminal modification is essential for export of the O-antigen across the inner membrane. WbdD is also required for correct localization of the WbdA mannosyltransferase.