Difference between revisions of "MleA"

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<pubmed> 16788182 22383849 22900538 11914346</pubmed>
'''Additional publications:''' {{PubMed|22383849}}
<pubmed> 16788182 22900538 11914346 23136871</pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 12:07, 10 November 2012

  • Description: malic enzyme

Gene name mleA
Synonyms yqkJ
Essential no
Product NAD-dependent malate dehydrogenase
Function malate utilization
Gene expression levels in SubtiExpress: mleA
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 45 kDa, 4.895
Gene length, protein length 1317 bp, 439 aa
Immediate neighbours yqkK, mleN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MleA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MleA expression.png

Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AnsR regulon, CcpA regulon

The gene

Basic information

  • Locus tag: BSU23550

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: (S)-malate + NAD+ = pyruvate + CO2 + NADH (according to Swiss-Prot) malate --> pyruvate
  • Protein family: malic enzymes family (according to Swiss-Prot)
  • Paralogous protein(s): YtsJ

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant: GP1136 (cat) available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks


Additional publications: PubMed

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)

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Guillaume Lerondel, Thierry Doan, Nicola Zamboni, Uwe Sauer, Stéphane Aymerich
YtsJ has the major physiological role of the four paralogous malic enzyme isoforms in Bacillus subtilis.
J. Bacteriol.: 2006, 188(13);4727-36
[PubMed:16788182] [WorldCat.org] [DOI] (P p)

Susan H Fisher, Lewis V Wray
Bacillus subtilis 168 contains two differentially regulated genes encoding L-asparaginase.
J. Bacteriol.: 2002, 184(8);2148-54
[PubMed:11914346] [WorldCat.org] [DOI] (P p)