Phospholipid-requiring bacterial enzyme. II. Role of phospholipid in the uridine diphosphate galactose: lipopolysaccharide α-3-galactosyl transferase reaction

Biochemistry ◽  
1969 ◽  
Vol 8 (9) ◽  
pp. 3508-3515 ◽  
Author(s):  
Akira Endo ◽  
Lawrence Rothfield

1974 ◽  
Vol 143 (3) ◽  
pp. 587-590 ◽  
Author(s):  
Barry J. Kitchen ◽  
Patrick Andrews

The inhibition of lactose synthetase A protein by p-hydroxymercuribenzoate at pH7.5 and 25°C, which involves the reaction of one molecule of inhibitor with each molecule of enzyme, was decreased in rate by UDP-galactose, especially in the presence of Mn2+. Pseudo-first-order rate constants for the reaction between 0.1mm-p-hydroxymercuribenzoate and free enzyme, the enzyme–UDP-galactose complex and the enzyme–Mn2+–UDP-galactose complex were 4.4×10−2, 1.9×10−2 and 0.3×10−2min−1 respectively. The results also indicated that dissociation constants for UDP-galactose in the enzyme–UDP-galactose and enzyme–Mn2+–UDP-galactose complexes were 313 and 16μm respectively, the latter value being similar to the Km for UDP-galactose in the lactose synthetase reaction. The protective effect of UDP-galactose and the role of Mn2+ ions in lactose synthetase are discussed.





1972 ◽  
Vol 247 (4) ◽  
pp. 1339-1342
Author(s):  
Timple G. Wee ◽  
Janet Davis ◽  
Perry A. Frey


1986 ◽  
Vol 144 (3) ◽  
pp. 150-151 ◽  
Author(s):  
Francis G. Bowling ◽  
David K.B. Fraser ◽  
Alan E. Clague ◽  
Darryl J. Morris ◽  
Alan Hayes




Sign in / Sign up

Export Citation Format

Share Document