RacE

• Description: glutamate racemase
  
  

Gene name	racE
Synonyms	glr
Essential	yes PubMed
Product	glutamate racemase
Function	peptidoglycan precursor biosynthesis
Gene expression levels in SubtiExpress: racE
Metabolic function and regulation of this protein in SubtiPathways: racE
MW, pI	29 kDa, 4.858
Gene length, protein length	816 bp, 272 aa
Immediate neighbours	gerM, ysmB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes

The gene

Basic information

• Locus tag: BSU28390

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU28390

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-glutamate = D-glutamate (according to Swiss-Prot)

• Protein family: aspartate/glutamate racemases family (according to Swiss-Prot)

• Paralogous protein(s): YrpC

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU28390

• Structure: 1ZUW (with D-glutamate)

• UniProt: P94556

• KEGG entry: [2]

• E.C. number: 5.1.1.3

Expression and regulation

• Operon: ysmB-racE PubMed

• Expression browser: racE PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 531 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Katie L Whalen, Anthony C Chau, M Ashley Spies
In silico optimization of a fragment-based hit yields biologically active, high-efficiency inhibitors for glutamate racemase.
ChemMedChem: 2013, 8(10);1681-9
[PubMed:23929705] [WorldCat.org] [DOI] (I p)

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

M Ashley Spies, Joseph G Reese, Dylan Dodd, Katherine L Pankow, Steven R Blanke, Jerome Baudry
Determinants of catalytic power and ligand binding in glutamate racemase.
J Am Chem Soc: 2009, 131(14);5274-84
[PubMed:19309142] [WorldCat.org] [DOI] (I p)

Eduard Puig, Edgar Mixcoha, Mireia Garcia-Viloca, Angels González-Lafont, José M Lluch
How the substrate D-glutamate drives the catalytic action of Bacillus subtilis glutamate racemase.
J Am Chem Soc: 2009, 131(10);3509-21
[PubMed:19227983] [WorldCat.org] [DOI] (I p)

Sergey N Ruzheinikov, Makie A Taal, Svetlana E Sedelnikova, Patrick J Baker, David W Rice
Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery.
Structure: 2005, 13(11);1707-13
[PubMed:16271894] [WorldCat.org] [DOI] (P p)

Keitarou Kimura, Lam-Son Phan Tran, Yoshifumi Itoh
Roles and regulation of the glutamate racemase isogenes, racE and yrpC, in Bacillus subtilis.
Microbiology (Reading): 2004, 150(Pt 9);2911-2920
[PubMed:15347750] [WorldCat.org] [DOI] (P p)