Difference between revisions of "LeuB"

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<pubmed>15060025,12193635,19258532,8289305,18641142,15547269,12618455,22517742,15547269,12618455,12107147, 20935095 24163341 15378759</pubmed>
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<pubmed>15060025,12193635,19258532,8289305,18641142,15547269,12618455,22517742,15547269,12618455,12107147, 20935095 25157083 24163341 15378759</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:37, 19 September 2014

  • Description: 3-isopropylmalate dehydrogenase

Gene name leuB
Synonyms leuC
Essential no
Product 3-isopropylmalate dehydrogenase
Function biosynthesis of leucine
Gene expression levels in SubtiExpress: leuB
Metabolic function and regulation of this protein in SubtiPathways:
leuB
MW, pI 39 kDa, 4.744
Gene length, protein length 1095 bp, 365 aa
Immediate neighbours leuC, leuA
Sequences Protein DNA DNA_with_flanks
Genetic context
LeuB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LeuB expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

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

The gene

Basic information

  • Locus tag: BSU28270

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 + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH (according to Swiss-Prot)
  • Protein family: LeuB type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylated on Arg-4 PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1XAD (Thermus thermophilus)
  • KEGG entry: [3]

Additional information

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
  • Additional information:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 6438 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 942 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5218 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2316 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1868 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References