New UDP-GlcNAc C4 Epimerase Involved in the Biosynthesis of 2-Acetamino-2-deoxy-l-altruronic Acid in the O-Antigen Repeating Units of Plesiomonas shigelloides O17
Abstract
Plesiomonas shigelloides is a ubiquitous waterborne pathogen responsible for diseases such as diarrhea and bacillary dysentery, commonly afflicting infants and children. This bacterium is endowed with an O-antigen gene cluster consisting of 10 consecutive reading frames. One of these, designated wbgU (orf3), has been overexpressed and biochemically characterized to show that it encodes a uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) C4 epimerase, only the second microbial enzyme characterized to have this activity. Epimerization is an equilibrium reaction resulting in a 70:30 ratio of UDP-GlcNAc to uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc), irrespective of the initial substrate. The K(m) values for UDP-GalNAc and UDP-GlcNAc are 131 microM and 137 microM, respectively. WbgU is also capable of converting nonacetylated derivatives but with much lower efficiency. It contains a tightly bound nicotinamide adenine dinucleotide [NAD(H)] molecule and requires no other cofactors for activity. We propose here that this enzyme catalyzes the first of the three transformations in the biosynthetic pathway of 2-acetamino-2-deoxy-L-altruronic acid, an unusual sugar present in the O-specific side chains of lipopolysaccharide of P. shigelloides O17 and its close relative Escherichia coli Sonnei.
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These results correlate with data previously published for the His-tagged 4-epimerase WbgU recombinantly expressed in E. coli BL21(DE3).
“These results also correlate with data previously published for the His-tagged 4-epimerase WbgU recombinantly expressed in E. coli BL21(DE3) [17].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [17]
In the cited paper, Km values of 0.13 mM are reported for both substrates.
“In the cited paper Km values of 0.13 mM are reported for both substrates.”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [17]
WbgU exhibits the highest activity at 37 °C.
“However, it has already been shown by Kowal and Wang, that WbgU exhibits the highest activity at 37 °C [17].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [17]
WbgU was chosen based on the well-characterized properties of the enzyme.
“WbgU was chosen based on the well-characterized properties of the enzyme [17].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [17]
At substrate saturation (1.5 mM), reaction velocities are different with the respective starting substrate.
“At substrate saturation (1.5 mM), reaction velocities are different with the respective starting substrate [17].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [17]
The authors have described a slower conversion rate of UDP-GlcNAc than that of UDP-GalNAc based on time course experiments using multiple enzyme dilutions.
“The authors have described a slower conversion rate of UDP-GlcNAc than that of UDP-GalNAc based on time course experiments using multiple enzyme dilutions [17].”
From High level in vivo mucin-type glycosylation in Escherichia coli (2018) · cites this paper as [17]
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High level in vivo mucin-type glycosylation in Escherichia coli
Mueller, P., Gauttam, R., Raab, N., Handrick, R., Wahl, C., Leptihn, S., Zorn, M., Kussmaul, M., Scheffold, M., Eikmanns, B., et al. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-1013-9 · Cited by 22 · see citing works
- Authors
- Kowal, P., & Wang, P. G.
- Affiliations
- Department of Chemistry, Wayne State University, Detroit, Michigan 48202
- Wayne State University (US)
- Corresponding author
- Wang, Peng George
- ORCID
- Wang, Peng George
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-11-21
- Volume
- 41
- Issue
- 51
- Pages
- 15410-15414
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2076400489
- Cited by
- 30
- References
- 0
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2018: 4 · 2017: 1 · 2015: 1 · 2012: 3
- FWCI
- 1.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI044040, AI 44040)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
- Keywords
- O-antigen biosynthesis, UDP-GalNAc, NAD-dependent enzyme, epimerization, bacterial polysaccharide biosynthesis
- MeSH terms
- Carbohydrate Epimerases, Chemistry, Physical, Enzyme Activation, Kinetics, Lipopolysaccharides, NAD, Oligosaccharides, Polysaccharides, Bacterial, Recombinant Proteins, Substrate Specificity, Uridine Diphosphate N-Acetylgalactosamine, Uridine Diphosphate N-Acetylglucosamine, Uronic Acids, Plesiomonas, Electrophoresis, Capillary, O Antigens, Chemical Phenomena
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