Catalysis of an Essential Step in Vitaminâ
B2 Biosynthesis by a Consortium of Broad Spectrum Hydrolases.
Chembiochem
; 16(17): 2466-9, 2015 Nov.
Article
em En
| MEDLINE
| ID: mdl-26316208
ABSTRACT
An enzyme catalysing the essential dephosphorylation of the riboflavin precursor, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate (6), was purified about 800-fold from a riboflavin-producing Bacillus subtilis strain, and was assigned as the translation product of the ycsE gene by mass spectrometry. YcsE is a member of the large haloacid dehalogenase (HAD) superfamily. The recombinant protein was expressed in Escherichia coli. It catalyses the hydrolysis of 6 (vmax , 12â
µmol mg(-1) min(-1) ; KM , 54â
µm) and of FMN (vmax , 25â
µmol mg(-1) min(-1) ; KM , 135â
µm). A ycsE deletion mutant of B.â
subtilis was not riboflavin dependent. Two additional proteins (YwtE, YitU) that catalyse the hydrolysis of 6 at appreciable rates were identified by screening 13 putative HAD superfamily members from B.â
subtilis. The evolutionary processes that have resulted in the handling of an essential step in the biosynthesis of an essential cofactor by a consortium of promiscuous enzymes require further analysis.
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Base de dados:
MEDLINE
Assunto principal:
Riboflavina
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article