Journal
CHEMBIOCHEM
Volume 16, Issue 17, Pages 2466-2469Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201500352
Keywords
biosynthesis; haloacid dehalogenase; hydrolases; isoenzymes; vitamin B-2
Ask authors/readers for more resources
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 (v(max), 12 mu molmg(-1) min(-1); K-M, 54 mu m) and of FMN (v(max), 25 mmolmg(-1)min(-1); K-M, 135 mu m). A ycsE deletion mutant of B. 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. 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available