The Enzyme Database

Your query returned 5 entries.    printer_iconPrintable version

EC 1.1.1.136     
Accepted name: UDP-N-acetylglucosamine 6-dehydrogenase
Reaction: UDP-N-acetyl-α-D-glucosamine + 2 NAD+ + H2O = UDP-2-acetamido-2-deoxy-α-D-glucuronate + 2 NADH + 2 H+
For diagram of UDP-N-acetylgalactosamine and UDP-N-acetylmannosamine biosynthesis, click here
Other name(s): uridine diphosphoacetylglucosamine dehydrogenase; UDP-acetylglucosamine dehydrogenase; UDP-2-acetamido-2-deoxy-D-glucose:NAD oxidoreductase; UDP-GlcNAc dehydrogenase; WbpA; WbpO
Systematic name: UDP-N-acetyl-α-D-glucosamine:NAD+ 6-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-83-5
References:
1.  Fan, D.-F., John, C.E., Zalitis, J. and Feingold, D.S. UDPacetylglucosamine dehydrogenase from Achromobacter georgiopolitanum. Arch. Biochem. Biophys. 135 (1969) 45–49. [DOI] [PMID: 4312076]
2.  Miller, W.L., Wenzel, C.Q., Daniels, C., Larocque, S., Brisson, J.R. and Lam, J.S. Biochemical characterization of WbpA, a UDP-N-acetyl-D-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 279 (2004) 37551–37558. [DOI] [PMID: 15226302]
[EC 1.1.1.136 created 1972, modified 2012]
 
 
EC 1.1.1.335     
Accepted name: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Reaction: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-α-D-ribo-hex-3-uluronate + NADH + H+
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Other name(s): WlbA; WbpB
Systematic name: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate:NAD+ 3-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. 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. J. Biol. Chem. 284 (2009) 11854–11862. [DOI] [PMID: 19282284]
2.  Larkin, A. and 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 48 (2009) 5446–5455. [DOI] [PMID: 19348502]
3.  Thoden, J.B. and Holden, H.M. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 49 (2010) 7939–7948. [DOI] [PMID: 20690587]
4.  Thoden, J.B. and Holden, H.M. 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 50 (2011) 1483–1491. [DOI] [PMID: 21241053]
[EC 1.1.1.335 created 2012]
 
 
EC 2.3.1.201     
Accepted name: UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase
Reaction: acetyl-CoA + UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate = CoA + UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Other name(s): WbpD; WlbB
Systematic name: acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate N-acetyltransferase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. 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. J. Biol. Chem. 284 (2009) 11854–11862. [DOI] [PMID: 19282284]
2.  Larkin, A. and 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 48 (2009) 5446–5455. [DOI] [PMID: 19348502]
[EC 2.3.1.201 created 2012]
 
 
EC 2.6.1.98     
Accepted name: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase
Reaction: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate + 2-oxoglutarate = UDP-2-acetamido-2-deoxy-α-D-ribo-hex-3-uluronate + L-glutamate
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Other name(s): WbpE; WlbC
Systematic name: UDP-2-acetamido-3-amino-2,3-dideoxy-α-D-glucuronate:2-oxoglutarate aminotransferase
Comments: A pyridoxal 5′-phosphate protein. This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the previous enzyme in the pathway, EC 1.1.1.335 (UDP-N-acetyl-2-amino-2-deoxyglucuronate oxidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. 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. J. Biol. Chem. 284 (2009) 11854–11862. [DOI] [PMID: 19282284]
2.  Larkin, A. and 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 48 (2009) 5446–5455. [DOI] [PMID: 19348502]
3.  Larkin, A., Olivier, N.B. and Imperiali, B. Structural analysis of WbpE from Pseudomonas aeruginosa PAO1: a nucleotide sugar aminotransferase involved in O-antigen assembly. Biochemistry 49 (2010) 7227–7237. [DOI] [PMID: 20604544]
[EC 2.6.1.98 created 2012]
 
 
EC 5.1.3.23     
Accepted name: UDP-2,3-diacetamido-2,3-dideoxyglucuronic acid 2-epimerase
Reaction: UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronate = UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronate
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Glossary: UDP-α-D-GlcNAc3NAcA = UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid
UDP-α-D-ManNAc3NAcA = UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid
Other name(s): UDP-GlcNAc3NAcA 2-epimerase; UDP-α-D-GlcNAc3NAcA 2-epimerase; 2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerase; WbpI; WlbD
Systematic name: 2,3-diacetamido-2,3-dideoxy-α-D-glucuronate 2-epimerase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of the B-band lipopolysaccharide of Pseudomonas aeroginosa serotype O5 and of the band-A trisaccharide of Bordetella pertussis, both important respiratory pathogens [1]. The enzyme is highly specific as UDP-α-D-GlcNAc, UDP-α-D-GlcNAcA (UDP-2-acetamido-2-deoxy-α-D-glucuronic acid) and UDP-α-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucose) cannot act as substrates [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Westman, E.L., McNally, D.J., Rejzek, M., Miller, W.L., Kannathasan, V.S., Preston, A., Maskell, D.J., Field, R.A., Brisson, J.R. and Lam, J.S. Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 123–130. [DOI] [PMID: 17346239]
2.  Westman, E.L., McNally, D.J., Rejzek, M., Miller, W.L., Kannathasan, V.S., Preston, A., Maskell, D.J., Field, R.A., Brisson, J.R. and Lam, J.S. Erratum report: Identification and biochemical characterization of two novel UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 625.
3.  Sri Kannathasan, V., Staines, A.G., Dong, C.J., Field, R.A., Preston, A.G., Maskell, D.J. and Naismith, J.H. Overexpression, purification, crystallization and data collection on the Bordetella pertussis wlbD gene product, a putative UDP-GlcNAc 2′-epimerase. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 1310–1312. [PMID: 11526328]
[EC 5.1.3.23 created 2007]
 
 


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