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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
- BsubCyc: BSU19630
- 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:
- Interactions:
- forms hexamers PubMed
- Localization:
- membrane (according to Swiss-Prot)
Database entries
- BsubCyc: BSU19630
- UniProt: O34925
- KEGG entry: [2]
- E.C. number: 2.4.2.1
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)