Difference between revisions of "PdhA"
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 {{PubMed|24696501}} | ** number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 {{PubMed|24696501}} | ||
** number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 {{PubMed|24696501}} | ** number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 {{PubMed|24696501}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4425 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5452 {{PubMed|21395229}} | ||
+ | ** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7055 {{PubMed|21395229}} | ||
=Biological materials = | =Biological materials = | ||
− | |||
* '''Mutant:''' | * '''Mutant:''' | ||
Revision as of 14:11, 17 April 2014
- Description: pyruvate dehydrogenase (E1 alpha subunit)
Gene name | pdhA |
Synonyms | aceA |
Essential | yes |
Product | pyruvate dehydrogenase (E1 alpha subunit) |
Function | links glycolysis and TCA cycle |
Gene expression levels in SubtiExpress: pdhA | |
Interactions involving this protein in SubtInteract: PdhA | |
Metabolic function and regulation of this protein in SubtiPathways: pdhA | |
MW, pI | 41 kDa, 5.837 |
Gene length, protein length | 1113 bp, 371 aa |
Immediate neighbours | ykyA, pdhB |
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
carbon core metabolism, essential genes, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14580
Phenotypes of a mutant
- pdhA is essential PubMed
Database entries
- BsubCyc: BSU14580
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2 (according to Swiss-Prot)
- Protein family:
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Modification:
- Cofactors:
- thiamine pyrophosphate
- Effectors of protein activity:
- Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
- Low sensibility to NADPH
Database entries
- BsubCyc: BSU14580
- Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus)
- UniProt: P21881
- KEGG entry: [3]
- E.C. number: 1.2.4.1
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- stringent response: due to presence of guanine at +1 position of the transcript PubMed
- Additional information:
- The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
- belongs to the 100 most abundant proteins PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium): 5117 PubMed
- number of protein molecules per cell (complex medium with amino acids, without glucose): 18311 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4425 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5452 PubMed
- number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7055 PubMed
Biological materials
- Mutant:
- Expression vector:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Arthur Aronson, Purdue University, West Lafayette, USA homepage
Your additional remarks
References
Reviews
Kai Tittmann
Reaction mechanisms of thiamin diphosphate enzymes: redox reactions.
FEBS J: 2009, 276(9);2454-68
[PubMed:19476487]
[WorldCat.org]
[DOI]
(I p)
U Neveling, S Bringer-Meyer, H Sahm
Gene and subunit organization of bacterial pyruvate dehydrogenase complexes.
Biochim Biophys Acta: 1998, 1385(2);367-72
[PubMed:9655937]
[WorldCat.org]
[DOI]
(P p)
M S Patel, T E Roche
Molecular biology and biochemistry of pyruvate dehydrogenase complexes.
FASEB J: 1990, 4(14);3224-33
[PubMed:2227213]
[WorldCat.org]
[DOI]
(P p)
P A Frey
Mechanism of coupled electron and group transfer in Escherichia coli pyruvate dehydrogenase.
Ann N Y Acad Sci: 1982, 378;250-64
[PubMed:6805383]
[WorldCat.org]
[DOI]
(P p)
Original publications