Difference between revisions of "PdhD"
(→References) |
|||
| Line 98: | Line 98: | ||
* '''Sigma factor:''' | * '''Sigma factor:''' | ||
| − | ** ''[[pdhA]]'': [[SigA]] {{PubMed| | + | ** ''[[pdhA]]'': [[SigA]] {{PubMed|20081037}} |
** ''[[pdhC]]'': [[SigA]] {{PubMed|11976308}} | ** ''[[pdhC]]'': [[SigA]] {{PubMed|11976308}} | ||
| − | * '''Regulation:''' expression activated by glucose (2.0 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed] | + | * '''Regulation:''' |
| + | ** ''[[pdhA]]'': expression activated by glucose (2.0-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:''' | ||
| Line 126: | Line 129: | ||
=References= | =References= | ||
| − | + | ==Reviews== | |
| − | <pubmed>12850135 6414463 11976308 17726680 </pubmed> | + | <pubmed> 19476487 9655937 </pubmed> |
| + | ==Original publications== | ||
| + | <pubmed>12850135 6414463 11976308 17726680 20081037 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 19:11, 19 January 2010
- 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 |
| Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
| 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
| |
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:
- 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)
- UniProt: P21880
- KEGG entry: [3]
- E.C. number: 1.8.1.4
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:
- 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
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)
Original publications
Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1573-85
[PubMed:20081037]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
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)
Haichun Gao, Xin Jiang, Kit Pogliano, Arthur I Aronson
The E1beta and E2 subunits of the Bacillus subtilis pyruvate dehydrogenase complex are involved in regulation of sporulation.
J Bacteriol: 2002, 184(10);2780-8
[PubMed:11976308]
[WorldCat.org]
[DOI]
(P p)
P N Lowe, J A Hodgson, R N Perham
Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in Bacillus subtilis.
Biochem J: 1983, 215(1);133-40
[PubMed:6414463]
[WorldCat.org]
[DOI]
(P p)
