Mdh

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU29120

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• Swiss prot entry: P49814

• KEGG entry: [3]

• E.C. number: 1.1.1.37

Additional information

The enzyme is a tetramer PubMed

Expression and regulation

• Operon:
  • citZ-icd-mdh
  • icd-mdh

• Sigma factor: SigA

• 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:

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