Difference between revisions of "TenA"

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==Original publications==
 
==Original publications==
<pubmed>15709744,18054064,17618314,,16356850, </pubmed>
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<pubmed>15709744,18054064,17618314,,16356850, 24311574</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:45, 8 December 2013

  • Description: thiaminase II

Gene name tenA
Synonyms
Essential no
Product thiaminase II
Function thiamine salvage
Gene expression levels in SubtiExpress: tenA
Metabolic function and regulation of this protein in SubtiPathways:
Thiamin
MW, pI 27 kDa, 4.99
Gene length, protein length 708 bp, 236 aa
Immediate neighbours yjbQ, tenI
Sequences Protein DNA DNA_with_flanks
Genetic context
TenA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TenA expression.png




























Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

Thi-box

The gene

Basic information

  • Locus tag: BSU11650

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole (according to Swiss-Prot)
  • Protein family: thiaminase-2 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

  • Structure: 1YAF, 2QCX (complex with formyl aminommethyl pyrimidine)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • 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

Reviews

T P Begley, D M Downs, S E Ealick, F W McLafferty, A P Van Loon, S Taylor, N Campobasso, H J Chiu, C Kinsland, J J Reddick, J Xi
Thiamin biosynthesis in prokaryotes.
Arch Microbiol: 1999, 171(5);293-300
[PubMed:10382260] [WorldCat.org] [DOI] (P p)

Original publications

Afshan Begum, Julia Drebes, Alexey Kikhney, Ingrid B Müller, Markus Perbandt, Dmitri Svergun, Carsten Wrenger, Christian Betzel
Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases.
Acta Crystallogr D Biol Crystallogr: 2013, 69(Pt 12);2320-9
[PubMed:24311574] [WorldCat.org] [DOI] (I p)

Amy L Jenkins, Yang Zhang, Steven E Ealick, Tadhg P Begley
Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.
Bioorg Chem: 2008, 36(1);29-32
[PubMed:18054064] [WorldCat.org] [DOI] (I p)

Amy Haas Jenkins, Ghislain Schyns, Sébastien Potot, Guangxing Sun, Tadhg P Begley
A new thiamin salvage pathway.
Nat Chem Biol: 2007, 3(8);492-7
[PubMed:17618314] [WorldCat.org] [DOI] (P p)

Narasimhan Sudarsan, Smadar Cohen-Chalamish, Shingo Nakamura, Gail Mitchell Emilsson, Ronald R Breaker
Thiamine pyrophosphate riboswitches are targets for the antimicrobial compound pyrithiamine.
Chem Biol: 2005, 12(12);1325-35
[PubMed:16356850] [WorldCat.org] [DOI] (P p)

Angela V Toms, Amy L Haas, Joo-Heon Park, Tadhg P Begley, Steven E Ealick
Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II.
Biochemistry: 2005, 44(7);2319-29
[PubMed:15709744] [WorldCat.org] [DOI] (P p)