Difference between revisions of "Mdh"

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(Biological materials)
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 936 bp, 312 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 936 bp, 312 aa  
 
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[icd]], [[phoP]]''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[phoP]], [[icd]]''
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14872&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB14872&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''

Revision as of 09:17, 7 December 2009

  • 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, 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
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)
    • repressed in the presence of glucose and glutamate (CcpC) PubMed

mdh: constitutive

  • Regulatory mechanism: CcpA: transcription repression, CcpC: transcription repression
    • CcpC: transcription repression (molecular inducer: citrate) PubMed
  • 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)
    • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP385, 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)

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)

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)