Difference between revisions of "TrpB"
| Line 58: | Line 58: | ||
=== Additional information=== | === Additional information=== | ||
| − | |||
| − | |||
| Line 84: | Line 82: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| − | * '''Interactions:''' [[TrpA]]-[[TrpB]] | + | * '''[[SubtInteract|Interactions]]:''' [[TrpA]]-[[TrpB]] |
| − | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
| Line 109: | Line 107: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
| − | ** induction by tryptophan ([[MtrB| TRAP]]) {{PubMed|1551827}} | + | ** induction by tryptophan ([[MtrB|TRAP]]) {{PubMed|1551827}} |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | ** [[MtrB| TRAP]]: binding to the mRNA in the presence of tryptophan, this results in transcription termination {{PubMed|8419914}} | + | ** [[MtrB|TRAP]]: binding to the mRNA in the presence of tryptophan, this results in transcription termination {{PubMed|8419914}} |
* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
=Biological materials = | =Biological materials = | ||
| Line 138: | Line 137: | ||
<pubmed> 18486479 11893063 11163353 7900177 19387555 </pubmed> | <pubmed> 18486479 11893063 11163353 7900177 19387555 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| + | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
| + | <big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> | ||
| + | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
| + | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
<pubmed> 14976255, 3924737, 6436812,2422155,8419914, 1551827, 17507374 </pubmed> | <pubmed> 14976255, 3924737, 6436812,2422155,8419914, 1551827, 17507374 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 18:28, 19 November 2011
- 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
| |
Contents
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: BSU22640
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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:
Database entries
- Structure:
- UniProt: P07600
- KEGG entry: [3]
- E.C. number: 4.2.1.20
Additional information
Expression and regulation
- Operon:
- Regulatory mechanism:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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
