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GDP-mannose and UDP-mannose (each at less than 1 micrometer) markedly inhibit glucosyl transfer from UDP-glucose (1.6 micrometer( to dolichyl phosphate in liver microsomal preparations. The biphasic response suggests the presence of two glucosyl transferases only one of which is inhibited. The inhibition appears to be a property of the intact nucleotide phosphate sugars and not due to competition for a limited pool of dolichyl phosphate. UDP-galactose and UDP-xylose cause a less marked inhibition of the same enzyme. The failure of UDP-glucose to inhibit mannosyl transfer suggests that the pool of dolichol monophosphate used by mannosyl transferase is not available to the glucosyl transferase. The relationship between the degree to which an exogenous prenol phosphate acts as an acceptor of mannose and the degree to which it inhibits mannosylation of endogenous dolichyl monophosphate varies among different prenyl phosphates. Mannosyl transferase exhibits two pH optima.
A K Kerr, and
F W Hemming
June 1986,
Carbohydrate research,
A K Kerr, and
F W Hemming
September 1984,
European journal of biochemistry,
A K Kerr, and
F W Hemming
March 1982,
Proceedings of the National Academy of Sciences of the United States of America,
A K Kerr, and
F W Hemming
February 1973,
Carbohydrate research,
A K Kerr, and
F W Hemming
March 1979,
FEBS letters,
A K Kerr, and
F W Hemming
November 1979,
FEBS letters,
A K Kerr, and
F W Hemming
February 1983,
The Biochemical journal,
A K Kerr, and
F W Hemming
June 1965,
Biochemical and biophysical research communications,
A K Kerr, and
F W Hemming
July 1980,
Biochemical and biophysical research communications,
A K Kerr, and
F W Hemming
March 1980,
The Biochemical journal,
