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Journal of Bacteriology, April 2008, p. 2615-2618, Vol. 190, No. 7
0021-9193/08/$08.00+0     doi:10.1128/JB.01900-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of an Archaeon-Specific Riboflavin Kinase{triangledown}

Zahra Mashhadi,1 Hong Zhang,2 Huimin Xu,1 and Robert H. White1*

Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061,1 Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 753902

Received 4 December 2007/ Accepted 25 January 2008

The riboflavin kinase in Methanocaldococcus jannaschii has been identified as the product of the MJ0056 gene. Recombinant expression of the MJ0056 gene in Escherichia coli led to a large increase in the amount of flavin mononucleotide (FMN) in the E. coli cell extract. The unexpected features of the purified recombinant enzyme were its use of CTP as the phosphoryl donor and the absence of a requirement for added metal ion to catalyze the formation of FMN. Identification of this riboflavin kinase fills another gap in the archaeal flavin biosynthetic pathway. Some divalent metals were found to be potent inhibitors of the reaction. The enzyme represents a unique CTP-dependent family of kinases.

* Corresponding author. Mailing address: Department of Biochemistry (0308), Virginia Polytechnic Institute and State University, Blacksburg, VA 24061. Phone: (540) 231-6605. Fax: (540) 231-9070. E-mail: rhwhite{at}vt.edu

{triangledown} Published ahead of print on 1 February 2008.

Journal of Bacteriology, April 2008, p. 2615-2618, Vol. 190, No. 7
0021-9193/08/$08.00+0     doi:10.1128/JB.01900-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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