Difference between revisions of "PdhD"
Cadu Cunha (talk | contribs) (→Phenotypes of a mutant) |
Cadu Cunha (talk | contribs) (→Extended information on the protein) |
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=== Extended information on the protein === | === Extended information on the protein === | ||
| − | * '''Kinetic information:''' | + | * '''Kinetic information:''' Michaelis-Menten [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed] |
* '''Domains:''' | * '''Domains:''' | ||
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* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| + | ** Inhibited thiamine 2-thiothiazolone diphosphate and NADH [http://www.ncbi.nlm.nih.gov/pubmed/6414463 PubMed] | ||
| + | ** Low sensibility to NADPH | ||
* '''Interactions:''' [[OdhA]]-[[OdhB]]-[[PdhD]], [[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]] | * '''Interactions:''' [[OdhA]]-[[OdhB]]-[[PdhD]], [[PdhA]]-[[PdhB]]-[[PdhC]]-[[PdhD]] | ||
Revision as of 14:09, 10 June 2009
- Description: dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes
| Gene name | pdhD |
| Synonyms | citL |
| Essential | no |
| Product | dihydrolipoamide dehydrogenase E3 subunit of both pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes |
| Function | links glycolysis and TCA cycle, enzyme in TCA cycle |
| MW, pI | 49 kDa, 4.76 |
| Gene length, protein length | 1410 bp, 470 aa |
| Immediate neighbours | pdhC, slp |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU14610
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: Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH (according to Swiss-Prot)
- Protein family: class-I pyridine nucleotide-disulfide oxidoreductase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Michaelis-Menten PubMed
- Domains:
- Modification: phosphorylated (Ser/Thr/Tyr) PubMed
- Cofactor(s):
- Effectors of protein activity:
- Inhibited thiamine 2-thiothiazolone diphosphate and NADH PubMed
- Low sensibility to NADPH
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure: 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus), 1EBD (complex with binding domain of dihydrolipoamide acetylase, Geobacillus stearothermophilus)
- Swiss prot entry: P21880
- KEGG entry: [3]
- E.C. number: 1.8.1.4
Additional information
Expression and regulation
- Sigma factor: SigA
- Regulation: expression activated by glucose (2.0 fold) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- 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
Your additional remarks
References
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
- Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
- Gao et al. (2002) The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation.J. Bacteriol. 184: 2780-2788. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
