Salmonella typhimurium molecular weight

Fig. 31.2. Agarose gel electrophoresis of doubly labeled PCR product (lane 2) obtained from Salmonella enterica serovar Typhimurium ATCC 14028 with the doubly labeled primer set IS200. Lane 3 Molecular weight marker (OX174-Hinf I genome). No band was obtained with sterile water used as a negative PCR control (lane 1).

Peterson, A.A., McGroarty, E.J. High-molecular-weight components in lipopolysaccharides of Salmonella typhimurium, Salmonella minnesota, and Escherichia coli. J Bacteriol 162 (1985) 738-745. 

Cystathionine-y-synthase isolated from Salmonella typhimurium is a tetramer (molecular weight 160000) and catalyses, in vivo, the y-replacement of O-suc-cinylhomoserine with cysteine [79] to yield cystathionine. The latter, by way of homocysteine, is involved in the biosynthesis of methionine. In other species of bacteria and plants the succinyl moiety may be replaced by acetyl, phosphoryl, or malonyl moieties [80]. In the absence of cysteine the enzyme catalyses an abnormal reaction resulting in the formation of a-oxobutyrate. The latter reaction has been utilised for mechanistic investigations pertinent to the y-eUmination-deamination process (vide infra). 

Phosphoribosyl formylglycineamidine synthetase catalyzes the irreversible transfer of the amide group of glutamine to phosphoribosyl formylglycineamide to form the corresponding amidine. The molecular weight of the Salmonella typhimurium and chicken liver enzymes is 135,000 21). 

The crystal structures of two representative small sialidases, with molecular weights around 40 kDa, have been determined one from Salmonella typhimurium [17] and one from Micromonospora viridifaciens [I8j. These reveal the same P-propeller fold seen in the influenza virus neuraminidase (Figure 2), despite having no sequence similarity to the viral enzyme, and not containing any disulphide bonds in contrast to the seven conserved disulfides in the viral enzyme. 

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