Difference between revisions of "PdhB"
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* '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}} | * '''Operon:''' ''[[pdhA]]-[[pdhB]]-[[pdhC]]-[[pdhD]]'' {{PubMed|11976308}} | ||
− | * '''Sigma factor:''' [[SigA]] {{PubMed| | + | * '''Sigma factor:''' [[SigA]] {{PubMed|20081037}} |
− | * '''Regulation:''' expression activated by glucose (2.8 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | + | * '''Regulation:''' |
+ | ** expression activated by glucose (2.8-fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | ||
+ | ** subject to negative stringent control upon amino acid limitation {{PubMed|20081037}} | ||
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
+ | ** stringent response: due to presence of guanine at +1 position of the transcript {{PubMed|20081037}} | ||
* '''Additional information:''' | * '''Additional information:''' |
Revision as of 18:51, 19 January 2010
- Description: pyruvate dehydrogenase (E1 beta subunit)
Gene name | pdhB |
Synonyms | |
Essential | no |
Product | pyruvate dehydrogenase (E1 beta subunit) |
Function | links glycolysis and TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 35 kDa, 4.547 |
Gene length, protein length | 975 bp, 325 aa |
Immediate neighbours | pdhA, pdhC |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU14590
Phenotypes of a mutant
- defects in sporulation and unable to grow on glucose as single carbon source PubMed
Database entries
- 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:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Domains:
- Modification: phosphorylation on (Ser-302 OR Ser-306) PubMed
- Cofactor(s):
- Effectors of protein activity:
- Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
- Low sensibility to NADPH
- Localization: membrane associated PubMed
Database entries
- Structure: 1W88 (E1 in complex with subunit binding domain of E2, Geobacillus stearothermophilus)
- UniProt: P21882
- 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:
Biological materials
- Mutant: GP459 (spc), available in Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Arthur Aronson, Purdue University, West Lafayette, USA homepage
Your additional remarks
References