LeuC

• Description: 3-isopropylmalate dehydratase (large subunit)
  
  

Gene name	leuC
Synonyms
Essential	no
Product	3-isopropylmalate dehydratase (large subunit)
Function	biosynthesis of leucine
MW, pI	52 kDa, 6.127
Gene length, protein length	1416 bp, 472 aa
Immediate neighbours	leuD, leuB
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: BSU28260

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H₂O (according to Swiss-Prot)

• Protein family: LeuC type 1 subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:

• Swiss prot entry: P80858

• KEGG entry: [3]

• E.C. number: 4.2.1.33

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: ilvB-ilvH-ilvC-leuA-leuB-leuC-leuD PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • repressed by casamino acids PubMed
  • expressed in the absence of branched-chain amino acids (BCAA)
  • expression is stimulated in the presence of glucose PubMed
  • repressed by CodY PubMed
  • less expressed under conditions of extreme iron limitation (FsrA) PubMed

• Regulatory mechanism:
  • TnrA: transcription repression PubMed
  • CodY: transcription repression PubMed
  • CodY: transcription repression PubMed
  • glucose regulation: CcpA PubMed
  • repression by BCAA: tRNA-controlled RNA switch (T-box) that mediates termination/antitermination
  • FsrA: translational repression PubMed

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Shigeo Tojo, Takenori Satomura, Kaori Morisaki, Ken-Ichi Yoshida, Kazutake Hirooka, Yasutaro Fujita
Negative transcriptional regulation of the ilv-leu operon for biosynthesis of branched-chain amino acids through the Bacillus subtilis global regulator TnrA.
J Bacteriol: 2004, 186(23);7971-9
[PubMed:15547269] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

1. Mäder et al. (2002) Transcriptome and Proteome Analysis of Bacillus subtilis Gene Expression Modulated by Amino Acid Availability. J. Bacteriol 184: 1844288-4295 PubMed
2. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed