Characterization of the pyrophosphate-dependent 6-phosphofructokinase from Methylococcus capsulatus Bath

Reshetnikov, AS, Rozova, ON, Khmelenina, VN, Mustakhimov, Ildar I., Beschastny, AP, Murrell, JC and Trotsenko, YA (2008) Characterization of the pyrophosphate-dependent 6-phosphofructokinase from Methylococcus capsulatus Bath. FEMS Microbiology Letters, 288 (2). pp. 202-210. ISSN 1574-6968

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An active pyrophosphate-dependent 6-phosphofructokinase (PPi-PFK) from the thermotolerant methanotroph Methylococcus capsulatus Bath, containing a six-residue polyhistidine tag, was characterized. The enzyme was homodimeric (2 × 45 kDa), nonallosteric and most active at pH 7.0. PPi-PFK catalyzed reactions of PPi-dependent phosphorylation of fructose-6-phosphate (F-6-P) (Km 2.27 mM and Vmax 7.6 U mg-1 of protein), sedoheptulose-7-phosphate (Km 0.027 mM and Vmax 31 U mg-1) and ribulose-5-phosphate. In the reaction with F-6-P, the apparent Km for PPi was 0.027 mM, while in the reverse reaction, Km for orthophosphate was 8.69 mM and that for fructose-1,6-bisphosphate 0.328 mM (Vmax 9.0 U mg-1). Phylogenetically, M. capsulatus PPi-PFK was most similar to PPi-PFKs from the lithoautotrophic ammonia oxidizers Nitrosomonas europaea (74.0%), Nitrosospira multiformis (73.6%) and Betaproteobacterial methylotroph Methylibium petroleiphilum PM1 (71.6% identity). Genes coding PPi-PFK and a putative V-type H+-translocating pyrophosphatase (H+-PPi-ase) were cotranscribed as an operon. The potential significance of the PPi-PFK for regulation of carbon and energy fluxes in M. capsulatus Bath is discussed.

Item Type: Article
Faculty \ School: Faculty of Science > School of Environmental Sciences
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Depositing User: Rhiannon Harvey
Date Deposited: 27 Mar 2012 17:14
Last Modified: 17 Oct 2018 11:30
DOI: 10.1111/j.1574-6968.2008.01366.x

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