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Biosynthesis of riboflavin. Characterization of the product of the deaminase.

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Biosynthesis of riboflavin. Characterization of the product of the deaminase. / Nielsen, Peter; Bacher, A.

in: BBA-BIOMEMBRANES, Jahrgang 662, Nr. 2, 2, 1981, S. 312-317.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Nielsen, P & Bacher, A 1981, 'Biosynthesis of riboflavin. Characterization of the product of the deaminase.', BBA-BIOMEMBRANES, Jg. 662, Nr. 2, 2, S. 312-317. <http://www.ncbi.nlm.nih.gov/pubmed/7317443?dopt=Citation>

APA

Nielsen, P., & Bacher, A. (1981). Biosynthesis of riboflavin. Characterization of the product of the deaminase. BBA-BIOMEMBRANES, 662(2), 312-317. [2]. http://www.ncbi.nlm.nih.gov/pubmed/7317443?dopt=Citation

Vancouver

Nielsen P, Bacher A. Biosynthesis of riboflavin. Characterization of the product of the deaminase. BBA-BIOMEMBRANES. 1981;662(2):312-317. 2.

Bibtex

@article{5273b6aa0c074841b79fd2a3055978ab,
title = "Biosynthesis of riboflavin. Characterization of the product of the deaminase.",
abstract = "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.",
author = "Peter Nielsen and A Bacher",
year = "1981",
language = "Deutsch",
volume = "662",
pages = "312--317",
journal = "BBA-BIOMEMBRANES",
issn = "0005-2736",
publisher = "Elsevier",
number = "2",

}

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 -