Difference between revisions of "AlsS"

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Revision as of 08:27, 31 August 2012

  • Description: acetolactate synthase

Gene name alsS
Synonyms
Essential no
Product acetolactate synthase
Function overflow metabolism
Gene expression levels in SubtiExpress: alsS
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 61 kDa, 5.164
Gene length, protein length 1713 bp, 571 aa
Immediate neighbours alsD, alsR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AlsS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AlsS2 expression.png



















Categories containing this gene/protein

carbon core metabolism

This gene is a member of the following regulons

AlsR regulon, Rex regulon, stringent response

The gene

Basic information

  • Locus tag: BSU36010

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 2 pyruvate = 2-acetolactate + CO2 (according to Swiss-Prot)
  • Protein family: TPP enzyme family (according to Swiss-Prot)

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • induction by acetate (AlsR) PubMed
    • repressed as long as terminal electron acceptors are available for respiration (Rex) PubMed
    • subject to positive stringent control upon lysine starvation PubMed

Note: since acetate formation requires ackA activation by CcpA there is an indirect effect of CcpA on the alsSD operon: the operon is not expressed in ccpA mutants

  • Regulatory mechanism:
    • stringent response: due to presence of adenines at +1 and +2 positions of the transcript PubMed
    • AlsR: transcription activation in the presence of acetate PubMed
    • Rex: transcription repression if the ratio NADH2/NAD is high PubMed
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Shigeo Tojo, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Heavy involvement of stringent transcription control depending on the adenine or guanine species of the transcription initiation site in glucose and pyruvate metabolism in Bacillus subtilis.
J Bacteriol: 2010, 192(6);1573-85
[PubMed:20081037] [WorldCat.org] [DOI] (I p)

Shota Atsumi, Zhen Li, James C Liao
Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli.
Appl Environ Microbiol: 2009, 75(19);6306-11
[PubMed:19684168] [WorldCat.org] [DOI] (I p)

Susana Romero-Garcia, Claudia Hernández-Bustos, Enrique Merino, Guillermo Gosset, Alfredo Martinez
Homolactic fermentation from glucose and cellobiose using Bacillus subtilis.
Microb Cell Fact: 2009, 8;23
[PubMed:19383131] [WorldCat.org] [DOI] (I e)

Takashi Inaoka, Takenori Satomura, Yasutaro Fujita, Kozo Ochi
Novel gene regulation mediated by overproduction of secondary metabolite neotrehalosadiamine in Bacillus subtilis.
FEMS Microbiol Lett: 2009, 291(2);151-6
[PubMed:19087206] [WorldCat.org] [DOI] (I p)

Heike Reents, Richard Münch, Thorben Dammeyer, Dieter Jahn, Elisabeth Härtig
The Fnr regulon of Bacillus subtilis.
J Bacteriol: 2006, 188(3);1103-12
[PubMed:16428414] [WorldCat.org] [DOI] (P p)

A J Turinsky, T R Moir-Blais, F J Grundy, T M Henkin
Bacillus subtilis ccpA gene mutants specifically defective in activation of acetoin biosynthesis.
J Bacteriol: 2000, 182(19);5611-4
[PubMed:10986270] [WorldCat.org] [DOI] (P p)

M C Renna, N Najimudin, L R Winik, S A Zahler
Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin.
J Bacteriol: 1993, 175(12);3863-75
[PubMed:7685336] [WorldCat.org] [DOI] (P p)