Difference between revisions of "Mdh"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:14, 17 March 2010
- Description: malate dehydrogenase
Gene name | mdh |
Synonyms | citH |
Essential | no |
Product | malate dehydrogenase |
Function | TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 33 kDa, 4.727 |
Gene length, protein length | 936 bp, 312 aa |
Immediate neighbours | phoP, icd |
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: BSU29120
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: (S)-malate + NAD+ = oxaloacetate + NADH (according to Swiss-Prot)
- Protein family: MDH type 3 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten PubMed
- Domains:
- Modification: phosphorylation on Ser-149 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot), membrane associated PubMed
Database entries
- Structure: 1EMD (E.coli)
- UniProt: P49814
- KEGG entry: [3]
- E.C. number: 1.1.1.37
Additional information
The enzyme is a tetramer PubMed
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP719 (spc), 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:
Labs working on this gene/protein
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)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
Hyun-Jin Kim, Agnes Roux, Abraham L Sonenshein
Direct and indirect roles of CcpA in regulation of Bacillus subtilis Krebs cycle genes.
Mol Microbiol: 2002, 45(1);179-90
[PubMed:12100558]
[WorldCat.org]
[DOI]
(P p)
C Jourlin-Castelli, N Mani, M M Nakano, A L Sonenshein
CcpC, a novel regulator of the LysR family required for glucose repression of the citB gene in Bacillus subtilis.
J Mol Biol: 2000, 295(4);865-78
[PubMed:10656796]
[WorldCat.org]
[DOI]
(P p)
S Jin, M De Jesús-Berríos, A L Sonenshein
A Bacillus subtilis malate dehydrogenase gene.
J Bacteriol: 1996, 178(2);560-3
[PubMed:8550482]
[WorldCat.org]
[DOI]
(P p)
A K Tyagi, F A Siddiqui, T A Venkitasubramanian
Studies on the purification and characterization of malate dehydrogenase from Mycobacterium phlei.
Biochim Biophys Acta: 1977, 485(2);255-67
[PubMed:922015]
[WorldCat.org]
[DOI]
(P p)
A YOSHIDA
ENZYMIC PROPERTIES OF MALATE DEHYDROGENASE OF BACILLUS SUBTILIS.
J Biol Chem: 1965, 240;1118-24
[PubMed:14284712]
[WorldCat.org]
(P p)