Identification and characterization of an archaeon-specific riboflavin kinase

Zahra Mashhadi, Hong Zhang, Huimin Xu, Robert H. White

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)2615-2618
Number of pages4
JournalJournal of Bacteriology
Volume190
Issue number7
DOIs
StatePublished - Apr 2008

Fingerprint

riboflavin kinase
Flavin Mononucleotide
Cytidine Triphosphate
Archaea
Methanocaldococcus
Metals
Escherichia coli
Biosynthetic Pathways
Enzymes
Cell Extracts
Phosphotransferases
Ions
Gene Expression
Genes

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Identification and characterization of an archaeon-specific riboflavin kinase. / Mashhadi, Zahra; Zhang, Hong; Xu, Huimin; White, Robert H.

In: Journal of Bacteriology, Vol. 190, No. 7, 04.2008, p. 2615-2618.

Research output: Contribution to journalArticle

Mashhadi, Zahra ; Zhang, Hong ; Xu, Huimin ; White, Robert H. / Identification and characterization of an archaeon-specific riboflavin kinase. In: Journal of Bacteriology. 2008 ; Vol. 190, No. 7. pp. 2615-2618.
@article{2256d04ece8b460cbe279b48c9f50b72,
title = "Identification and characterization of an archaeon-specific riboflavin kinase",
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.",
author = "Zahra Mashhadi and Hong Zhang and Huimin Xu and White, {Robert H.}",
year = "2008",
month = "4",
doi = "10.1128/JB.01900-07",
language = "English (US)",
volume = "190",
pages = "2615--2618",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "7",

}

TY - JOUR

T1 - Identification and characterization of an archaeon-specific riboflavin kinase

AU - Mashhadi, Zahra

AU - Zhang, Hong

AU - Xu, Huimin

AU - White, Robert H.

PY - 2008/4

Y1 - 2008/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=41549136541&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=41549136541&partnerID=8YFLogxK

U2 - 10.1128/JB.01900-07

DO - 10.1128/JB.01900-07

M3 - Article

C2 - 18245297

AN - SCOPUS:41549136541

VL - 190

SP - 2615

EP - 2618

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 7

ER -