TrpB

• Description: tryptophan synthase (beta subunit)
  
  

Gene name	trpB
Synonyms
Essential	no
Product	tryptophan synthase (beta subunit)
Function	biosynthesis of tryptophan
Interactions involving this protein in SubtInteract: TrpB
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp
MW, pI	43 kDa, 5.526
Gene length, protein length	1200 bp, 400 aa
Immediate neighbours	trpA, trpF
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

• Locus tag: BSU22640

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H₂O (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: TrpA-TrpB

• Localization:

Database entries

• Structure:

• UniProt: P07600

• KEGG entry: [3]

• E.C. number: 4.2.1.20

Expression and regulation

• Operon:
  • aroF-aroB-aroH-trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE (according to DBTBS)
  • trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE PubMed

• Sigma factor:
  • trpE: SigA PubMed

• Regulation:
  • induction by tryptophan (TRAP) PubMed

• Regulatory mechanism:
  • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed

• Additional information:
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Samanta Raboni, Stefano Bettati, Andrea Mozzarelli
Tryptophan synthase: a mine for enzymologists.
Cell Mol Life Sci: 2009, 66(14);2391-403
[PubMed:19387555] [WorldCat.org] [DOI] (I p)

Michael F Dunn, Dimitri Niks, Huu Ngo, Thomas R M Barends, Ilme Schlichting
Tryptophan synthase: the workings of a channeling nanomachine.
Trends Biochem Sci: 2008, 33(6);254-64
[PubMed:18486479] [WorldCat.org] [DOI] (P p)

E W Miles
Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.
Chem Rec: 2001, 1(2);140-51
[PubMed:11893063] [WorldCat.org] [DOI] (P p)

N K Nagradova
Interdomain interactions in oligomeric enzymes: creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers.
FEBS Lett: 2001, 487(3);327-32
[PubMed:11163353] [WorldCat.org] [DOI] (P p)

E W Miles
Tryptophan synthase. Structure, function, and protein engineering.
Subcell Biochem: 1995, 24;207-54
[PubMed:7900177] [WorldCat.org] (P p)

Original publications

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947