Document Detail

Possibility of 2,4,5-triamino-6-hydroxypyrimidine as an intermediate in the pathway of riboflavin biosynthesis.
MedLine Citation:
PMID:  4041122     Owner:  NLM     Status:  MEDLINE    
It was studied with resting cells of a high flavinogenic mold, Eremothecium ashbyii, whether or not 2,4,5-triamino-6-hydroxypyrimidine (THP) is an intermediate in the early pathway of riboflavin biosynthesis. A small amounts of THP strongly inhibited riboflavin formation in the resting cells, but the inhibition was effectively reversed by the added purines, except for adenine. Radioactive tracer experiments showed that the incorporation of the radioactivity from [2-14C]THP into riboflavin was negligible. The results obtained strongly suggest that THP is not an intermediate but a rigid inhibitor for riboflavin formation, and thus there is non salvage pathway of THP for the pathway of riboflavin biosynthesis in resting cells of E. ashbyii.
K Nakajima; Y Yamada; H Mitsuda
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Acta vitaminologica et enzymologica     Volume:  7     ISSN:  0300-8924     ISO Abbreviation:  Acta Vitaminol. Enzymol.     Publication Date:  1985  
Date Detail:
Created Date:  1985-10-09     Completed Date:  1985-10-09     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  0135063     Medline TA:  Acta Vitaminol Enzymol     Country:  ITALY    
Other Details:
Languages:  eng     Pagination:  19-24     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Ascomycota / metabolism*
Carbon Radioisotopes
Pyrimidines / metabolism*
Riboflavin / biosynthesis*
Saccharomycetales / metabolism*
Reg. No./Substance:
0/Carbon Radioisotopes; 0/Pyrimidines; 1004-75-7/6-hydroxy-2,4,5-triaminopyrimidine; 83-88-5/Riboflavin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  A case of primary malignant lymphoma of the urinary bladder
Next Document:  Studies on the 4-carbon compound needed for the formation of the O-xylene ring of riboflavin.