Difference between revisions of "Mdh"

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{{SubtiWiki category|[[carbon core metabolism]]}},
 
{{SubtiWiki category|[[carbon core metabolism]]}},
 
{{SubtiWiki category|[[membrane proteins]]}},
 
{{SubtiWiki category|[[membrane proteins]]}},
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{{SubtiWiki category|[[phosphoproteins]]}}
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{{SubtiWiki category|[[phosphoproteins]]}},
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[[most abundant proteins]]
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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* '''Additional information:'''
 
* '''Additional information:'''
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** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
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<pubmed>10656796,18763711 14284712 922015 12100558 17218307 8550482 8045899 20933603 22517742 23136871 24325460 24571712</pubmed>
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<pubmed>10656796,18763711 14284712 922015 12100558 17218307 8550482 8045899 20933603 22517742 23136871 24325460 15378759 24571712</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:00, 5 March 2014

  • Description: malate dehydrogenase

Gene name mdh
Synonyms citH
Essential no
Product malate dehydrogenase
Function TCA cycle
Gene expression levels in SubtiExpress: mdh
Interactions involving this protein in SubtInteract: Mdh
Metabolic function and regulation of this protein in SubtiPathways:
mdh
MW, pI 33 kDa, 4.727
Gene length, protein length 936 bp, 312 aa
Immediate neighbours phoP, icd
Sequences Protein DNA DNA_with_flanks
Genetic context
Mdh context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Mdh expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CcpA regulon, CcpC regulon

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
    • specific activity: 0.56 µmol min-1 (mg protein)-1 PubMed
  • Modification:
    • phosphorylated on Arg-156 PubMed
    • phosphorylation on Ser-149 PubMed
  • 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

Database entries

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

Additional information

  • The enzyme is a tetramer PubMed
  • extensive information on the structure and enzymatic properties of Mdh can be found at Proteopedia

Expression and regulation

  • Regulatory mechanism:
    • CcpA: transcription repression, CcpC: transcription repression PubMed
    • CcpC: transcription repression (molecular inducer: citrate) PubMed

Biological materials

  • Expression vector:
    • pGP385: for expression, purification in E. coli with N-terminal His-tag, in pWH844, available in Jörg Stülke's lab
    • pGP1123 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Jörg Stülke's lab)
    • pGP1755 (expression / purification of Mdh-S149A, with N-terminal His-tag from E. coli, in pWH844), available in Jörg Stülke's lab
    • pGP1764 (for expression, purification in E. coli with N-terminal Strep-tag, in pGP172, available in Jörg Stülke's lab)
    • GP1438(mdh-Strep (spc)) & GP1440(mdh-Strep (cat)), purification from B. subtilis, for SPINE, available in Jörg Stülke's lab
  • lacZ fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Michael Kohlstedt, Praveen K Sappa, Hanna Meyer, Sandra Maaß, Adrienne Zaprasis, Tamara Hoffmann, Judith Becker, Leif Steil, Michael Hecker, Jan Maarten van Dijl, Michael Lalk, Ulrike Mäder, Jörg Stülke, Erhard Bremer, Uwe Völker, Christoph Wittmann
Adaptation of Bacillus subtilis carbon core metabolism to simultaneous nutrient limitation and osmotic challenge: a multi-omics perspective.
Environ Microbiol: 2014, 16(6);1898-917
[PubMed:24571712] [WorldCat.org] [DOI] (I p)

Maike Bartholomae, Frederik M Meyer, Fabian M Commichau, Andreas Burkovski, Wolfgang Hillen, Gerald Seidel
Complex formation between malate dehydrogenase and isocitrate dehydrogenase from Bacillus subtilis is regulated by tricarboxylic acid cycle metabolites.
FEBS J: 2014, 281(4);1132-43
[PubMed:24325460] [WorldCat.org] [DOI] (I p)

Frederik M Meyer, Jörg Stülke
Malate metabolism in Bacillus subtilis: distinct roles for three classes of malate-oxidizing enzymes.
FEMS Microbiol Lett: 2013, 339(1);17-22
[PubMed:23136871] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Frederik M Meyer, Jan Gerwig, Elke Hammer, Christina Herzberg, Fabian M Commichau, Uwe Völker, Jörg Stülke
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon.
Metab Eng: 2011, 13(1);18-27
[PubMed:20933603] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)

S Jin, A L Sonenshein
Transcriptional regulation of Bacillus subtilis citrate synthase genes.
J Bacteriol: 1994, 176(15);4680-90
[PubMed:8045899] [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)

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