Difference between revisions of "AroH"

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=References=
 
=References=
  
<pubmed>8378335, 25422475, </pubmed>
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<pubmed>8378335, 25422475, 12630863 10960481 2105742 8643526 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:31, 26 November 2014

  • Description: chorismate mutase (isozymes 1 and 2)

Gene name aroH
Synonyms
Essential no
Product chorismate mutase (isozymes 1 and 2)
Function biosynthesis of aromatic amino acids
Gene expression levels in SubtiExpress: aroH
Metabolic function and regulation of this protein in SubtiPathways:
aroH
MW, pI 14 kDa, 5.524
Gene length, protein length 381 bp, 127 aa
Immediate neighbours trpE, aroB
Sequences Protein DNA DNA_with_flanks
Genetic context
AroH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AroH expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU22690

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Chorismate = prephenate (according to Swiss-Prot)
  • Protein family: BCKDHA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
    • 2CHT (complex with a transition state analog)
    • 1DBF
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1441 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1006 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 804 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Daniel Burschowsky, André van Eerde, Mats Ökvist, Alexander Kienhöfer, Peter Kast, Donald Hilvert, Ute Krengel
Electrostatic transition state stabilization rather than reactant destabilization provides the chemical basis for efficient chorismate mutase catalysis.
Proc Natl Acad Sci U S A: 2014, 111(49);17516-21
[PubMed:25422475] [WorldCat.org] [DOI] (I p)

Alexander Kienhöfer, Peter Kast, Donald Hilvert
Selective stabilization of the chorismate mutase transition state by a positively charged hydrogen bond donor.
J Am Chem Soc: 2003, 125(11);3206-7
[PubMed:12630863] [WorldCat.org] [DOI] (P p)

P Kast, C Grisostomi, I A Chen, S Li, U Krengel, Y Xue, D Hilvert
A strategically positioned cation is crucial for efficient catalysis by chorismate mutase.
J Biol Chem: 2000, 275(47);36832-8
[PubMed:10960481] [WorldCat.org] [DOI] (P p)

P Kast, M Asif-Ullah, N Jiang, D Hilvert
Exploring the active site of chorismate mutase by combinatorial mutagenesis and selection: the importance of electrostatic catalysis.
Proc Natl Acad Sci U S A: 1996, 93(10);5043-8
[PubMed:8643526] [WorldCat.org] [DOI] (P p)

Y M Chook, H Ke, W N Lipscomb
Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog.
Proc Natl Acad Sci U S A: 1993, 90(18);8600-3
[PubMed:8378335] [WorldCat.org] [DOI] (P p)

J V Gray, B Golinelli-Pimpaneau, J R Knowles
Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli.
Biochemistry: 1990, 29(2);376-83
[PubMed:2105742] [WorldCat.org] [DOI] (P p)