Temperature dependence of membranous and solubilized sialyltransferase activities in the presence of 1-palmitoyl-sn-glycero-3-phosphorylcholine and fatty acids

The membrane-bound sialyltransferase obtained from Escherichia coli K-235 grown in a chemically defined medium (ideal for colominic acid production) was studied. The in vivo half-life calculated for this enzyme was 20 h. Kinetic tests revealed (at 33 "C and pH 8.3) hyperbolic behaviour with respect to CMP-NeuSAc (K, 250 pM) and a transition temperature at 31.3"C. The enzyme was inhibited by NH:, some divalent cations and by several agents that react with thiol groups. Detergents and fatty acids also inhibited the sialyltransferase activity. In vitro synthesis of colominic acid is strongly inhibited by CMP by blocking the incorporation of [ 14C]Neu5Ac into a protein-complex intermediate and therefore into free polymer. CDP and CTP also inhibited (91 YO and 84%) this enzyme activity whereas cytosine and cytidine had no effect. In Escherichia coli K-235 the synthesis and assembly of colominic acid (an a2+8 hoinopolymer of NeuSAc) has been shown to be mediated by a membrane-associated sialyltransferase complex which catalyzes the incorporation of sialic acid from CMP-Neu5Ac into polymeric products or into a lipid fraction [S, 9, 111. Although the biosynthesis of colominic acid has been extensively studied [6-121, little is known about the regulation and metabolic effectors involved Correspondence fo J. M. Luengo,

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Temperature dependence of membranous and solubilized sialyltransferase activities in the presence of 1-palmitoyl-sn-glycero-3-phosphorylcholine and fatty acids

Cited by 4 publications

References 36 publications

Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins.

Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins.

Purification and biochemical characterization of phenylacetyl-CoA ligase from Pseudomonas putida. A specific enzyme for the catabolism of phenylacetic acid.

In vitro synthesis of colominic acid by membrane‐bound sialyltransferase of Escherichia coli K‐235

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