Difference between revisions of "DeoD"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 457 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 457 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1533 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 1533 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2828 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2576 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3169 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:05, 17 April 2014

  • Description: purine nucleoside phosphorylase

Gene name deoD
Synonyms
Essential no
Product purine nucleoside phosphorylase
Function purine salvage and interconversion
Gene expression levels in SubtiExpress: deoD
Metabolic function and regulation of this protein in SubtiPathways:
deoD
MW, pI 25 kDa, 4.978
Gene length, protein length 699 bp, 233 aa
Immediate neighbours yodJ, yoyE
Sequences Protein DNA DNA_with_flanks
Genetic context
DeoD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DeoD expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, membrane proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU19630

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 457 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1533 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2828 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2576 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3169 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Priscila O de Giuseppe, Nadia H Martins, Andreia N Meza, Camila R dos Santos, Humberto D'Muniz Pereira, Mario T Murakami
Insights into phosphate cooperativity and influence of substrate modifications on binding and catalysis of hexameric purine nucleoside phosphorylases.
PLoS One: 2012, 7(9);e44282
[PubMed:22957058] [WorldCat.org] [DOI] (I p)

Haojian Li, Guoqiang Zhang, Aihua Deng, Ning Chen, Tingyi Wen
De novo engineering and metabolic flux analysis of inosine biosynthesis in Bacillus subtilis.
Biotechnol Lett: 2011, 33(8);1575-80
[PubMed:21424839] [WorldCat.org] [DOI] (I p)

Rosa Grenha, Vladimir M Levdikov, Mark J Fogg, Elena V Blagova, James A Brannigan, Anthony J Wilkinson, Keith S Wilson
Structure of purine nucleoside phosphorylase (DeoD) from Bacillus anthracis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2005, 61(Pt 5);459-62
[PubMed:16511068] [WorldCat.org] [DOI] (I p)