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Details for article 11 of 19 found articles
| Title: |
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. shermani |
| Author: |
Guillaume Meurice Catherine Deborde Daniel Jacob Hélène Falentin Patrick Boyaval Diliana Dimova |
| Appeared in: |
In silico biology |
| Paging: | Volume 4 (2005) nr. 4 pages 517-528 |
| Year: |
2005-02-28 |
| Contents: |
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. |
| Publisher: |
IOS Press |
| Source file: |
Elektronische Wetenschappelijke Tijdschriften |
Details for article 11 of 19 found articles
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