Autor: |
Bellion E, Kirkley DH, Faust JR |
Jazyk: |
angličtina |
Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1976 Jun 23; Vol. 437 (1), pp. 229-37. |
DOI: |
10.1016/0304-4165(76)90364-0 |
Abstrakt: |
The mechanism of biosynthesis of 4-methyl-5-beta-hydroxyethyl thiazole, the thiazole moiety of thiamine was studied in Salmonella typhimurium. Using the adenosine derepression technique the incorporation of various 14C-labeled precursors was determined. We found that;e1Me-14C]methionine, [2-14C]methionine, [U-14C]alanine, and [2-14C]glycine were not incorporated whereas [2-14C]tyrosine was incorporated. Degradation of the 4-methyl-5-beta-hydroxyethyl thiazole obtained after [2-14C]tyrosine incorporation revealed that all of the activity was located on carbon-2. These findings are discussed and compared with previous findings concerning 4-methyl-5-beta-hydroxyethyl thiazole biosynthesis. |
Databáze: |
MEDLINE |
Externí odkaz: |
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