Section 17
Chapter 16,697

Polyprenol phosphate as an acceptor of mannose from guanosine diphosphate mannose in Aspergillus niger

Barr, R.M.; Hemming, F.W.

Biochemical Journal 126(5): 1203-1208


ISSN/ISBN: 0264-6021
PMID: 5073732
DOI: 10.1042/bj1261203
Accession: 016696021

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Growth of Aspergillus niger in the presence of [2-(14)C]mevalonate and (32)P(i) led to the formation of a lipid, containing (14)C (0.14% of dose) and (32)P (0.009% of dose), that had chromatographic properties identical with those of exo-methylene-hexahydropolyprenol phosphate. When a particulate enzyme preparation from the thallus of A. niger was incubated with GDP-[(14)C]mannose, the main radioactive products were mannose 1-phosphate (57% of products) and mannose (18%). In addition radioactive mannan (8%) and a mannolipid (2%) were formed. The latter was identified as exo-methylene-hexahydropolyprenol phosphate mannose on the basis of its chromatographic properties, acid lability and on the increase in formation of the mannolipid when the phosphate of exo-methylene-hexahydropolyprenols was added to the incubation mixture. The phosphates of ficaprenols and cetyl alcohol caused no corresponding increase. These observations are interpreted as evidence that the thallus of A. niger contains a mannose transferase that uses the phosphate of exo-methylene-hexahydropolyprenols as an acceptor. This situation is discussed in the light of the analogous involvement of a prenol phosphate mannose as an intermediate in the biosynthesis of bacterial wall mannan.

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