Difference between revisions of "Cah"

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* '''Additional information:'''
 
* '''Additional information:'''
** number of protein molecules per cell (complex medium with amino acids, without glucose): 205 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 980 {{PubMed|21395229}}
 
  
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1680 {{PubMed|21395229}}
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=Biological materials =
  
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:43, 17 April 2014

  • Description: cephalosporin C deacetylase

Gene name cah
Synonyms
Essential no
Product cephalosporin C deacetylase)
Function resistance to cephalosporin C
Gene expression levels in SubtiExpress: cah
MW, pI 35 kDa, 5.419
Gene length, protein length 954 bp, 318 aa
Immediate neighbours ycgK, ycgL
Sequences Protein DNA DNA_with_flanks
Genetic context
Cah context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Cah expression.png
























Categories containing this gene/protein

resistance against toxins/ antibiotics

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU03180

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Deacetylation of xylans and xylo-oligosaccharides (according to Swiss-Prot)
  • Protein family: carbohydrate esterase 7 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • 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

A Takimoto, S Yagi, K Mitsushima
High-level expression, purification, and some properties of a recombinant cephalosporin-C deacetylase.
J Biosci Bioeng: 1999, 87(4);456-62
[PubMed:16232499] [WorldCat.org] [DOI] (P p)

Akio Takimoto, Tomoaki Takakura, Hiroyoshi Tani, Shigeo Yagi, Kenji Mitsushima
Batch production of deacetyl 7-aminocephalosporanic acid by immobilized cephalosporin-C deacetylase.
Appl Microbiol Biotechnol: 2004, 65(3);263-7
[PubMed:15069587] [WorldCat.org] [DOI] (P p)

Florence Vincent, Simon J Charnock, Koen H G Verschueren, Johan P Turkenburg, David J Scott, Wendy A Offen, Shirley Roberts, Gavin Pell, Harry J Gilbert, Gideon J Davies, James A Brannigan
Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution.
J Mol Biol: 2003, 330(3);593-606
[PubMed:12842474] [WorldCat.org] [DOI] (P p)

K Mitsushima, A Takimoto, T Sonoyama, S Yagi
Gene cloning, nucleotide sequence, and expression of a cephalosporin-C deacetylase from Bacillus subtilis.
Appl Environ Microbiol: 1995, 61(6);2224-9
[PubMed:7793942] [WorldCat.org] [DOI] (P p)