superpathway of UDP-N-acetylglucosamine-derived O-antigen building blocks biosynthesis

Larkin A, Imperiali B. The Expanding Horizons of Asparagine-Linked Glycosylation. Biochemistry. 2011 May 04;50(21):4411–26. doi: 10.1021/bi200346n.; Thoden JB, Holden HM. Biochemical and Structural Characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: Enzymes Required for the Biosynthesis of 2,3-Diacetamido-2,3-dideoxy-d-mannuronic Acid. Biochemistry. 2011 Feb 08;50(9):1483–91. doi: 10.1021/bi101871f.; Thoden JB, Holden HM. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid . Biochemistry. 2010 Sep 14;49(36):7939–48. PMID: 20690587; PMCID: PMC4241754.; Larkin A, Olivier NB, Imperiali B. Structural Analysis of WbpE from Pseudomonas aeruginosa PAO1: A Nucleotide Sugar Aminotransferase Involved in O-Antigen Assembly, Biochemistry. 2010 Jul 28;49(33):7227–37. doi: 10.1021/bi100805b.; Larkin A, Imperiali B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: Enzymes in the Wbp Pathway Responsible for O-Antigen Assembly in Pseudomonas aeruginosa PAO1. Biochemistry. 2009 May 22;48(23):5446–55. doi: 10.1021/bi900186u.; Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS. Characterization of WbpB, WbpE, and WbpD and Reconstitution of a Pathway for the Biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-d-mannuronic Acid in Pseudomonas aeruginosa. Journal of Biological Chemistry. 2009 May;284(18):11854–62. doi: 10.1074/jbc.m808583200.; King JD, Mulrooney EF, Vinogradov E, Kneidinger B, Mead K, Lam JS. lfnA from Pseudomonas aeruginosa O12 and wbuX from Escherichia coli O145 Encode Membrane-Associated Proteins and Are Required for Expression of 2,6-Dideoxy-2-Acetamidino- l -Galactose in Lipopolysaccharide O Antigen. J Bacteriol. 2008 Mar;190(5):1671–9. doi: 10.1128/jb.01708-07.; Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J Biol Chem. 2006 Jan 13;281(2):723–32. doi: 10.1074/jbc.m511021200. PMID: 16286454.; Samuel G, Reeves P. Biosynthesis of O-antigens: genes and pathways involved in nucleotide sugar precursor synthesis and O-antigen assembly. Carbohydr Res. 2003 Nov 14;338(23):2503–19. doi: 10.1016/j.carres.2003.07.009. PMID: 14670712.; Kneidinger B, O'Riordan K, Li J, Brisson JR, Lee JC, Lam JS. Three highly conserved proteins catalyze the conversion of UDP-N-acetyl-D-glucosamine to precursors for the biosynthesis of O antigen in Pseudomonas aeruginosa O11 and capsule in Staphylococcus aureus type 5. Implications for the UDP-N-acetyl-L-fucosamine biosynthetic pathway. J Biol Chem. 2003 Feb 07;278(6):3615–27. doi: 10.1074/jbc.m203867200. PMID: 12464616.; Bélanger M, Burrows LL, Lam JS. Functional analysis of genes responsible for the synthesis of the B-band O antigen of Pseudomonas aeruginosa serotype O6 lipopolysaccharide The GenBank accession number for the sequence reported in this paper is AF035937. 1999 Dec 01;145(12):3505–21. doi: 10.1099/00221287-145-12-3505.; Finck CM, Hodell MG, Marx WH, Paskanik AM, McGraw DJ, Lutz CJ, Gatto LA, Picone AL, Nieman GF. Endotoxin-stimulated alveolar macrophage recruitment of neutrophils and modulation with exogenous surfactant. Crit Care Med. 1998 Aug;26(8):1414–8. doi: 10.1097/00003246-199808000-00029. PMID: 9710102.; Oldendorf WH. NMR imaging: its potential clinical impact. Hosp Pract (Off Ed). 1982 Sep;17(9):114–28. doi: 10.1080/21548331.1982.11702372. PMID: 6286454.

Metabolites



Enzyme

EC Number name full name note
1.1.1.136 UDP-N-acetylglucosamine 6-dehydrogenase UDP-N-acetyl-alpha-D-glucosamine:NAD+ 6-oxidoreductase
1.1.1.335 UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase
1.1.1.336 UDP-N-acetyl-D-mannosamine dehydrogenase UDP-N-acetyl-alpha-D-mannosamine:NAD+ 6-oxidoreductase
2.3.1.157 glucosamine-1-phosphate N-acetyltransferase acetyl-CoA:alpha-D-glucosamine-1-phosphate N-acetyltransferase
2.3.1.201 UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate N-acetyltransferase
2.6.1.16 glutamine-fructose-6-phosphate transaminase (isomerizing) L-glutamine:D-fructose-6-phosphate isomerase (deaminating)
2.6.1.98 UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate:2-oxoglutarate aminotransferase
2.7.7.23 UDP-N-acetylglucosamine diphosphorylase UTP:N-acetyl-alpha-D-glucosamine-1-phosphate uridylyltransferase
5.1.3.14 UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) UDP-N-acetyl-alpha-D-glucosamine 2-epimerase
5.1.3.23 UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase 2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronate 2-epimerase
5.3.1.9 glucose-6-phosphate isomerase alpha-D-glucose-6-phosphate aldose-ketose-isomerase (configuration-inverting)
5.4.2.10 phosphoglucosamine mutase alpha-D-glucosamine 1,6-phosphomutase


Proteins

Protein ID name full name
G3XD01 wbpD UDP-2-acetamido-3-amino-2,3-dideoxy-d-glucuronic acid N-acetyltransferase, WbpD
G3XD23 wbpB UDP-2-acetamido-2-deoxy-d-glucuronic acid 3-dehydrogenase, WbpB
G3XD61 wbpI UDP-N-acetylglucosamine 2-epimerase WbpI
G3XD94 wbpA UDP-N-acetyl-d-glucosamine 6-Dehydrogenase
P0A6T1 pgi Glucose-6-phosphate isomerase
P0ACC7 glmU Bifunctional protein GlmU
P17169 glmS Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
P27828 wecB UDP-N-acetylglucosamine 2-epimerase
P27829 wecC UDP-N-acetyl-D-mannosamine dehydrogenase
P31120 glmM Phosphoglucosamine mutase
Q9HZ76 wbpE UDP-2-acetamido-2-dideoxy-d-ribo-hex-3-uluronic acid transaminase, wbpE
Q9RHD6 wbpP UDP-N-acetyl-alpha-D-glucosaminouronate 4-epimerase
Q9RHD7 wbpO UDP-N-acetyl-D-glucosamine 6-dehydrogenase