PMID:12083785
| Citation |
Hwang, TS, Hung, CH, Teo, CF, Chen, GT, Chang, LS, Chen, SF, Chen, YJ and Lin, CH (2002) Structural characterization of Escherichia coli sialic acid synthase. Biochem. Biophys. Res. Commun. 295:167-73 |
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| Abstract |
Sialic acid synthase encoded by the neuB gene of Escherichia coli catalyzes the condensation of N-acetylmannosamine and phosphoenolpyruvate to form N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD, MALDI-TOF, and chemical cross-linking studies. Also, a specific cleavage by endogenous protease(s) has been identified at Lys(280) of the enzyme (40 kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7 kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form, and alterations in both secondary and native quaternary structures. |
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| Keywords |
Aldehyde-Lyases/chemistry; Circular Dichroism; Escherichia coli/enzymology; Oxo-Acid-Lyases/chemistry; Oxo-Acid-Lyases/metabolism; Protein Conformation; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
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