Salmonella typhimurium neuraminidase acts with inversion of configuration.
When the time course of the hydrolysis of identical solutions of p-nitrophenyl N-acetyl-alpha-D-neuraminide by Salmonella typhimurium neuraminidase is monitored by u.v. and by its optical rotation, the rotation change is synchronous with, or even marginally in advance of, the absorbance change. In experiments under the same conditions with influenza-virus neuraminidase, known to react with retention of configuration [Chong, Pegg, Taylor and von Itzstein (1992) Eur. J. Biochem. 207, 335-343], the rotation change is much slower than the absorbance change. The inverting, presumably single-displacement, mode of action of the S. typhimurium enzyme follows from these observations, and the position (92.5% beta) of the slowly established mutarotational equilibrium of N-acetylneuraminic acid [Friebolin, Kunzelmann, Supp, Brossmer, Keilich and Ziegler (1981) Tetrahedron Lett. 22, 1383-1386].
Guo
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X
Department of Chemistry (M/C 111), University of Illinois at Chicago 60607-7061.
Sinnott
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ML
D007700:Kinetics; D008968:Molecular Conformation; D015394:Molecular Structure; D009439:Neuraminidase / Q000378:metabolism*; D009904:Optical Rotation; D009975:Orthomyxoviridae / Q000201:enzymology; D011994:Recombinant Proteins / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology*; D012794:Sialic Acids / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D013237:Stereoisomerism
D011994:Recombinant Proteins; D012794:Sialic Acids; C053158:2-O-(4-nitrophenyl)-N-acetylneuraminic acid; D009439:Neuraminidase