Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Bacteriol. 2008 Apr;190(7):2615-8. doi: 10.1128/JB.01900-07. Epub 2008 Feb 1.

Identification and characterization of an archaeon-specific riboflavin kinase.

Author information

  • 1Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061, USA.

Abstract

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.

PMID:
18245297
[PubMed - indexed for MEDLINE]
PMCID:
PMC2293203
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk