Difference between revisions of "LeuD"

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(References)
(Database entries)
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* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU28250&redirect=T BSU28250]
 
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU28250&redirect=T BSU28250]
  
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2PKP 2PKP] (from ''Methanocaldococcus jannaschii dsm 2661'', 38% identity, 53% similarity)  
+
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2hcu 2hcu] (from ''Streptococcus mutans'', 48% identity)  
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P94568 P94568]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P94568 P94568]

Revision as of 13:12, 30 July 2015

  • Description: 3-isopropylmalate dehydratase (small subunit)

Gene name leuD
Synonyms
Essential no
Product 3-isopropylmalate dehydratase (small subunit)
Function biosynthesis of leucine
Gene expression levels in SubtiExpress: leuD
Metabolic function and regulation of this protein in SubtiPathways:
leuD
MW, pI 22 kDa, 4.582
Gene length, protein length 597 bp, 199 aa
Immediate neighbours ysoA, leuC
Sequences Protein DNA DNA_with_flanks
Genetic context
LeuD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LeuD expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

CcpA regulon, CodY regulon, FsrA regulon, T-box, TnrA regulon

The gene

Basic information

  • Locus tag: BSU28250

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O (according to Swiss-Prot)
  • Protein family: LeuD type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2hcu (from Streptococcus mutans, 48% identity)
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • for a complete overview on the regulation of the ilv operon, see Brinsmade et al.
    • repressed by casamino acids PubMed
    • expression is stimulated in the presence of glucose PubMed
    • 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
    • less expressed under conditions of extreme iron limitation (FsrA) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1251 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5846 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 3609 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 2313 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References