학술논문
In Silico Exploration of the Fructose-6- Phosphate Phosphorylation Step in Glycolysis: Genomic Evidence of the Coexistence of an Atypical ATP-Dependent Along with a PPi-Dependent Phosphofructokinase in Propionibacterium freudenreichii subsp. shermanii.
Document Type
Article
Author
Source
Subject
*FRUCTOSE
*PHOSPHATES
*PHOSPHORYLATION
*GLYCOLYSIS
*PROPIONIBACTERIUM
*ADENOSINE triphosphate
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Language
ISSN
1386-6338
Abstract
We performed a detailed bioinformatic study of the catalytic step of fructose-6-phosphate phosphorylation in glycolysis based on the raw genomic draft of Propionibacterium freudenreichii subsp. shermanii (P. shermanii) ATCC9614 [Meurice et al., 2004]. Our results provide the first in silico evidence of the coexistence of genes coding for an ATP-dependent phosphofructokinase (ATP-PFK) and a PPi-dependent phosphofructokinase (PPi-PFK), whereas the fructose-1,6-bisphosphatase (FBP) and ADP-dependent phosphofructokinase (ADP-PFK) are absent. The deduced amino acid sequence corresponding to the PPi-PFK (AJ508922) shares 100% similarity with the already characterised propionibacterial protein (P29495; Ladror et al., 1991]. The unexpected ATP-PFK gene (AJ509827) encodes a protein of 373 aa which is highly similar (50% positive residues) along at least 95% of its sequence length to different well-characterised ATP-PFKs. The characteristic PROSITE pattern important for the enzyme function of ATP-PFKs (PS00433) was conserved in the putative ATP-PFK sequence: 8 outof. [ABSTRACT FROM AUTHOR]