Difference between revisions of "Icd"
(→Biological materials) |
Cadu Cunha (talk | contribs) (→Extended information on the protein) |
||
Line 61: | Line 61: | ||
=== Extended information on the protein === | === Extended information on the protein === | ||
− | * '''Kinetic information:''' | + | * '''Kinetic information:''' Reversible Michaelis-Menten [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed] |
* '''Domains:''' | * '''Domains:''' | ||
Line 70: | Line 70: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
+ | ** Inhibited by glyoxylate, oxaloacetate and oxalomalate [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed] | ||
+ | *** Better inhibition when glyoxylate and oxaloacetate is combined, probably due to the non-enzymatic conversion into oxalomalate, which is a strong inhibitor [http://www.ncbi.nlm.nih.gov/pubmed/4147570 PubMed] | ||
* '''Interactions:''' | * '''Interactions:''' |
Revision as of 15:21, 10 June 2009
- Description: isocitrate dehydrogenase
Gene name | icd |
Synonyms | citC |
Essential | no |
Product | isocitrate dehydrogenase |
Function | TCA cycle |
MW, pI | 46 kDa, 4.833 |
Gene length, protein length | 1269 bp, 423 aa |
Immediate neighbours | citZ, mdh |
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: BSU29130
Phenotypes of a mutant
reduced ability to sporulate PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH (according to Swiss-Prot)
- Protein family: isocitrate and isopropylmalate dehydrogenases family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten PubMed
- Domains:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: attached to the membrane PubMed
Database entries
- Structure: 1HQS
- Swiss prot entry: P39126
- KEGG entry: [3]
- E.C. number: 1.1.1.42 2
Additional information
Expression and regulation
- Sigma factor: SigA
- Regulation: repressed by glucose (2.2-fold) (CcpA) PubMed, citZ: catabolite repression (CcpA), repression by glucose + glutamate (CcpC)
icd: constitutive
- Regulatory mechanism: CcpA: transcription repression
- Additional information:
Biological materials
- Mutant: GP666 (spc), GP672 (erm), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Linc Sonenshein lab
Labs working on this gene/protein
[Linc Sonenshein|Linc Sonenshein]], Tufts University, Boston, MA, USA Homepage
Your additional remarks
References
Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711]
[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)
Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705]
[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)
Satinder K Singh, Stephen P Miller, Antony Dean, Leonard J Banaszak, David C LaPorte
Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/phosphatase.
J Biol Chem: 2002, 277(9);7567-73
[PubMed:11751849]
[WorldCat.org]
[DOI]
(P p)
K Matsuno, T Blais, A W Serio, T Conway, T M Henkin, A L Sonenshein
Metabolic imbalance and sporulation in an isocitrate dehydrogenase mutant of Bacillus subtilis.
J Bacteriol: 1999, 181(11);3382-91
[PubMed:10348849]
[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
- Matsuno K, Blais T, Serio AW, Conway T, Henkin TM, Sonenshein AL (1999) Metabolic imbalance and sporulation in an isocitrate dehydrogenase mutant of Bacillus subtilis. J Bacteriol 181:3382-3391. PubMed
- Singh SK, Miller SP, Dean A, Banaszak LJ, LaPorte DC (2002) Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for Escherichia coli isocitrate dehydrogenase kinase/ phosphatase. J Biol Chem 277: 7567-7573. PubMed
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Levine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6, 2157-2173. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed