Difference between revisions of "Mdh"

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(Additional information)
(References)
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<pubmed>18763711, </pubmed>
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<pubmed>18763711 14284712 922015 </pubmed>
 
# Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing ''Bacillus subtilis'' by divergent approaches. Proteomics '''8:''' 4123-4136 [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
 
# Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing ''Bacillus subtilis'' by divergent approaches. Proteomics '''8:''' 4123-4136 [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 10:40, 11 June 2009

  • Description: malate dehydrogenase

Gene name mdh
Synonyms citH
Essential no
Product malate dehydrogenase
Function TCA cycle
MW, pI 33 kDa, 4.727
Gene length, protein length 936 bp, 312 aa
Immediate neighbours icd, phoP
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Mdh context.gif
This image was kindly provided by SubtiList





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:
  • Cofactor(s):
  • Effectors of protein activity:
    • Inhibited by Mg2+, Ca2+, Zn2+, Ag2+ and Hg2+ PubMed PubMed
    • Inhibited by oxaloacetate (above 1mM) and malate (above 7,7mM) PubMed
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot), membrane associated PubMed


Database entries

  • Structure: 1EMD (E.coli)
  • KEGG entry: [3]

Additional information

The enzyme is a tetramer PubMed

Expression and regulation

  • Regulation: citZ: catabolite repression (CcpA), repression by glucose + glutamate (CcpC)

mdh: constitutive

  • Regulatory mechanism: CcpA: transcription repression, CcpC: transcription repression


  • Additional information:

Biological materials

  • Mutant: GP719 (spc), available in Stülke lab
  • Expression vector:
    • pGP1123 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Stülke lab)
  • 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)

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)

  1. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed