"Tryptophan Synthase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An enzyme that catalyzes the conversion of L-serine and 1-(indol-3-yl)glycerol 3-phosphate to L-tryptophan and glyceraldehyde 3-phosphate. It is a pyridoxal phosphate protein that also catalyzes the conversion of serine and indole into tryptophan and water and of indoleglycerol phosphate into indole and glyceraldehyde phosphate. (From Enzyme Nomenclature, 1992) EC 4.2.1.20.
| Descriptor ID |
D014367
|
| MeSH Number(s) |
D08.811.520.241.300.850 D08.811.600.896
|
| Concept/Terms |
Tryptophan Synthase- Tryptophan Synthase
- Synthase, Tryptophan
- Tryptophan Synthetase
- Synthetase, Tryptophan
|
Below are MeSH descriptors whose meaning is more general than "Tryptophan Synthase".
Below are MeSH descriptors whose meaning is more specific than "Tryptophan Synthase".
This graph shows the total number of publications written about "Tryptophan Synthase" by people in this website by year, and whether "Tryptophan Synthase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1999 | 5 | 0 | 5 |
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Below are the most recent publications written about "Tryptophan Synthase" by people in Profiles.
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Wu Y, Kondrashkina E, Kayatekin C, Matthews CR, Bilsel O. Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein. Proc Natl Acad Sci U S A. 2008 Sep 09; 105(36):13367-72.
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Wu Y, Vadrevu R, Kathuria S, Yang X, Matthews CR. A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein. J Mol Biol. 2007 Mar 09; 366(5):1624-38.
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Gualfetti PJ, Iwakura M, Lee JC, Kihara H, Bilsel O, Zitzewitz JA, Matthews CR. Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein. Biochemistry. 1999 Oct 05; 38(40):13367-78.
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Zitzewitz JA, Matthews CR. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein. Biochemistry. 1999 Aug 03; 38(31):10205-14.
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Gualfetti PJ, Bilsel O, Matthews CR. The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Sci. 1999 Aug; 8(8):1623-35.
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Zitzewitz JA, Gualfetti PJ, Perkons IA, Wasta SA, Matthews CR. Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein. Protein Sci. 1999 Jun; 8(6):1200-9.
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Bilsel O, Yang L, Zitzewitz JA, Beechem JM, Matthews CR. Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time. Biochemistry. 1999 Mar 30; 38(13):4177-87.
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Bilsel O, Zitzewitz JA, Bowers KE, Matthews CR. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry. 1999 Jan 19; 38(3):1018-29.