Biosynthesis of riboflavin. Characterization of the product of the deaminase.
Standard
Biosynthesis of riboflavin. Characterization of the product of the deaminase. / Nielsen, Peter; Bacher, A.
In: BBA-BIOMEMBRANES, Vol. 662, No. 2, 2, 1981, p. 312-317.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
Harvard
APA
Vancouver
Bibtex
}
RIS
TY - JOUR
T1 - Biosynthesis of riboflavin. Characterization of the product of the deaminase.
AU - Nielsen, Peter
AU - Bacher, A
PY - 1981
Y1 - 1981
N2 - The 2'5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate deaminase was partially purified from cell extracts of Candida guilliermondii ATCC 9058. The enzyme requires Mg2+ for activity. Maximal activity was observed at pH 7,3. The enzyme converts its substrate, 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate, to 2,5-diamino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate. This labile compound was treated with diacetyl and the resulting 6,7-dimethyl-8-ribityllumazine 5'-phosphate was identified by comparison with a synthetic sample.
AB - The 2'5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate deaminase was partially purified from cell extracts of Candida guilliermondii ATCC 9058. The enzyme requires Mg2+ for activity. Maximal activity was observed at pH 7,3. The enzyme converts its substrate, 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate, to 2,5-diamino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate. This labile compound was treated with diacetyl and the resulting 6,7-dimethyl-8-ribityllumazine 5'-phosphate was identified by comparison with a synthetic sample.
M3 - SCORING: Zeitschriftenaufsatz
VL - 662
SP - 312
EP - 317
JO - BBA-BIOMEMBRANES
JF - BBA-BIOMEMBRANES
SN - 0005-2736
IS - 2
M1 - 2
ER -