Pasteurella multocida sialic acid aldolase: A promising biocatalyst

Yanhong Li, Hai Yu, Hongzhi Cao, Kam Lau, Saddam Muthana, Vinod Kumar Tiwari, Bryan Son, Xi Chen

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


Sialic acid aldolases or N-acetylneuraminate lyases (NanAs) catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-d-mannosamine (ManNAc). A capillary electrophoresis assay was developed to directly characterize the activities of NanAs in both Neu5Ac cleavage and Neu5Ac synthesis directions. The assay was used to obtain the pH profile and the kinetic data of a NanA cloned from Pasteurella multocida P-1059 (PmNanA) and a previously reported recombinant Escherichia coli K12 NanA (EcNanA). Both enzymes are active in a broad pH range of 6.0-9.0 in both reaction directions and have similar kinetic parameters. Substrates specificity studies showed that 5-O-methyl-ManNAc, a ManNAc derivative, can be used efficiently as a substrate by PmNanA, but not efficiently by EcNanA, for the synthesis of 8-O-methyl Neu5Ac. In addition, PmNanA (250 mg l-1 culture) has a higher expression level (2.5-fold) than EcNanA (94 mg l -1 culture). The higher expression level and a broader substrate tolerance make PmNanA a better catalyst than EcNanA for the chemoenzymatic synthesis of sialic acids and their derivatives.

Original languageEnglish (US)
Pages (from-to)963-970
Number of pages8
JournalApplied Microbiology and Biotechnology
Issue number6
StatePublished - Jul 2008


  • Aldolase
  • Capillary electrophoresis
  • Escherichia coli
  • Lyase
  • NanA
  • Pasteurella multocida

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology
  • Bioengineering
  • Microbiology (medical)


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