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PMID:25799411

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Citation

Ji, W, Sun, W, Feng, J, Song, T, Zhang, D, Ouyang, P, Gu, Z and Xie, J (2015) Characterization of a novel N-acetylneuraminic acid lyase favoring N-acetylneuraminic acid synthesis. Sci Rep 5:9341

Abstract

N-Acetylneuraminic acid lyase (NAL, E.C. number 4.1.3.3) is a Class I aldolase that catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) from pyruvate and N-acetyl-D-mannosamine (ManNAc). Due to the equilibrium favoring Neu5Ac cleavage, the enzyme catalyzes the rate-limiting step of two biocatalytic reactions producing Neu5Ac in industry. We report the biochemical characterization of a novel NAL from a "GRAS" (General recognized as safe) strain C. glutamicum ATCC 13032 (CgNal). Compared to all previously reported NALs, CgNal exhibited the lowest kcat/Km value for Neu5Ac and highest kcat/Km values for ManNAc and pyruvate, which makes CgNal favor Neu5Ac synthesis the most. The recombinant CgNal reached the highest expression level (480 mg/L culture), and the highest reported yield of Neu5Ac was achieved (194 g/L, 0.63 M). All these unique properties make CgNal a promising biocatalyst for industrial Neu5Ac biosynthesis. Additionally, although showing the best Neu5Ac synthesis activity among the NAL family, CgNal is more related to dihydrodipicolinate synthase (DHDPS) by phylogenetic analysis. The activities of CgNal towards both NAL's and DHDPS' substrates are fairly high, which indicates CgNal a bi-functional enzyme. The sequence analysis suggests that CgNal might have adopted a unique set of residues for substrates recognition.

Links

PubMed Online version:10.1038/srep09341

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

CORGL:Q8NMD2

enables

GO:0008747: N-acetylneuraminate lyase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

CORGL:Q8NMD2

GO:0008747: N-acetylneuraminate lyase activity

ECO:0000314:

F

Table 1 shows the kinetic parameters for Neu5Ac cleavage and synthesis by CgNAL

complete
CACAO 10797

Notes

See also

References

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