ArticleApplied microbiology and biotechnology2014
Donor substrate promiscuity of the N-acetylglucosaminyltransferase activities of Pasteurella multocida heparosan synthase 2 (PmHS2) and Escherichia coli K5 KfiA.
Article in Applied microbiology and biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Advances in chemoenzymatic synthesis of glycosaminoglycans and proteoglycans.Current opinion in chemical biology · 2026Review
- Biosynthetic production of anticoagulant heparin polysaccharides through metabolic and sulfotransferases engineering strategies.Nature communications · 2024Article
- Novel β1,4 N-acetylglucosaminyltransferase in de novo enzymatic synthesis of hyaluronic acid oligosaccharides.Applied microbiology and biotechnology · 2023Article
- Imaging ofScience advances · 2023Article
- Enzymatic Synthesis of Glycans and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021Review
- EngineerACS catalysis · 2020Article
- Tools for Studying Glycans: Recent Advances in Chemoenzymatic Glycan Labeling.ACS chemical biology · 2017Review
- Uncovering the Catalytic Direction of Chondroitin AC Exolyase: FROM THE REDUCING END TOWARDS THE NON-REDUCING END.The Journal of biological chemistry · 2016Article
- Improved one-pot multienzyme (OPME) systems for synthesizing UDP-uronic acids and glucuronides.Chemical communications (Cambridge, England) · 2015Article
- Masquerading microbial pathogens: capsular polysaccharides mimic host-tissue molecules.FEMS microbiology reviews · 2014Review
- Tailored design and synthesis of heparan sulfate oligosaccharide analogues using sequential one-pot multienzyme systems.Angewandte Chemie (International ed. in English) · 2013Article
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8 authors.
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Abstract
The biological activities of heparan sulfate (HS) and heparin (HP) are closely related to their molecular structures. Both Pasteurella multocida heparosan synthase 2 (PmHS2) and Escherichia coli K5 KfiA have been used for enzymatic and chemoenzymatic synthesis of HS and HP oligosaccharides and their derivatives. We show here that cloning using the pET15b vector and expressing PmHS2 as an N-His6-tagged fusion protein improve its expression level in E. coli. Investigation of the donor substrate specificity of the N-acetylglucosaminyltransferase activities of P. multocida heparosan synthase 2 (PmHS2) and E. coli K5 KfiA indicates the substrate promiscuities of PmHS2 and KfiA. Overall, both PmHS2 and KfiA can use uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) and some of its C2'- and C6'-derivatives as donor substrates for their α1-4-GlcNAcT activities. Nevertheless, PmHS2 has a broader tolerance towards substrate modifications. Other than the UDP-sugars that can be used by KfiA, additional C6'-derivatives of UDP-GlcNAc, UDP-glucose, and UDP-N-acetylgalactosamine (UDP-GalNAc) are tolerable substrates for the α1-4-GlcNAcT activity of PmHS2. The substrate promiscuities of PmHS2 and KfiA will allow efficient chemoenzymatic synthesis of diverse HS and HP oligosaccharide derivatives which may have improved or altered activities compared to their natural counterparts.
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