Affordable Access

Access to the full text

Characterization of recombinant PPi-dependent 6-phosphofructokinases from Methylosinus trichosporium OB3b and Methylobacterium nodulans ORS 2060

Authors
  • Rozova, O. N.1
  • Khmelenina, V. N.1
  • Trotsenko, Y. A.1
  • 1 Russian Academy of Sciences, Skryabin Institute of Biochemistry and Physiology of Microorganisms, pr. Nauki 5, Pushchino, Moscow Region, 142290, Russia , Pushchino, Moscow Region (Russia)
Type
Published Article
Journal
Biochemistry (Moscow)
Publisher
Pleiades Publishing
Publication Date
Mar 16, 2012
Volume
77
Issue
3
Pages
288–295
Identifiers
DOI: 10.1134/S0006297912030078
Source
Springer Nature
Keywords
License
Yellow

Abstract

The properties of the purified recombinant PPi-dependent 6-phosphofructokinases (PPi-PFKs) from the methanotroph Methylosinus trichosporium OB3b and rhizospheric phytosymbiont Methylobacterium nodulans ORS 2060 were determined. The dependence of activities of PPi-PFK-His6-tag from Ms. trichosporium OB3b (6 × 45 kDa) and PPi-PFK from Mb. nodulans ORS 2060 (4 × 43 kDa) on the concentrations of substrates of forward and reverse reactions conformed to Michaelis-Menten kinetics. Besides fructose-6-phosphate, the enzymes also phosphorylated sedoheptulose-7-phosphate. ADP or AMP (1 mM each) inhibited activity of the Ms. trichosporium PPi-PFK but did not affect the activity of the Mb. nodulans enzyme. Preference of PPi-PFKs to fructose-1,6-bisphosphate implied a predominant function of the enzymes in hexose phosphate synthesis in these bacteria. PPi-PFKs from the methylotrophs have low similarity of translated amino acid sequences (17% identity) and belong to different phylogenetic subgroups of type II 6-phosphofructokinases. The relationship of PPi-PFKs with microaerophilic character of Ms. trichosporium OB3b and adaptation of Mb. nodulans ORS 2060 to anaerobic phase of phytosymbiosis are discussed.

Report this publication

Statistics

Seen <100 times