Subunits: Beta Subunit, Alpha Subunit with PLP, IGP
Identifiers
EC no.
4.2.1.20
CAS no.
9014-52-2
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Gene Ontology
AmiGO / QuickGO
Search
PMC
articles
PubMed
articles
NCBI
proteins
Tryptophan synthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyzes the final two steps in the biosynthesis of tryptophan.[1][2] It is commonly found in Eubacteria,[3] Archaebacteria,[4] Protista,[5] Fungi,[6] and Plantae.[7] However, it is absent from Animalia.[8] It is typically found as an α2β2 tetramer.[9][10] The α subunits catalyze the reversible formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Each α active site is connected to a β active site by a 25 Ångstrom long hydrophobic channel contained within the enzyme. This facilitates the diffusion of indole formed at α active sites directly to β active sites in a process known as substrate channeling.[11] The active sites of tryptophan synthase are allosterically coupled.[12]
^Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I (June 2008). "Tryptophan synthase: the workings of a channeling nanomachine". Trends in Biochemical Sciences. 33 (6): 254–64. doi:10.1016/j.tibs.2008.04.008. PMID 18486479.
^Miles EW (1991). "Structural basis for catalysis by tryptophan synthase". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology and Related Areas of Molecular Biology. Vol. 64. pp. 93–172. doi:10.1002/9780470123102.ch3. ISBN 9780470123102. PMID 2053470.
^Jablonski P, Jablonski L, Pintado O, Sriranganathan N, Howde C (September 1996). "Tryptophan synthase: Identification of Pasteurella multocida tryptophan synthase B-subunit by antisera against strain PI059". Microbiology. 142: 115–21. doi:10.1099/13500872-142-1-115. PMID 8581158.
^Lazcano A, Diaz-Villgomez E, Mills T, Oro J (March 1995). "On the levels of enzymatic substrate specificity: Implications for the early evolution of metabolic pathways". Advances in Space Research. 15 (3): 345–56. doi:10.1016/S0273-1177(99)80106-9. PMID 11539248.
^Anderson I, Watkins R, Samuelson J, Spencer D, Majoros W, Grey M, Loftus B (August 2005). "Gene Discovery in the Acanthamoeba castellanii Genome". Protist. 156 (2): 203–14. doi:10.1016/j.protis.2005.04.001. PMID 16171187.
^Ireland C, Peekhaus N, Lu P, Sangari R, Zhang A, Masurekar P, An Z (April 2008). "The tryptophan synthetase gene TRP1 of Nodulisporium sp.: molecular characterization and its relation to nodulisporic acid A production". Appl Microbiol Biotechnol. 79 (3): 451–9. doi:10.1007/s00253-008-1440-3. PMID 18389234. S2CID 7230896.
^Sanjaya, Hsiao PY, Su RC, Ko SS, Tong CG, Yang RY, Chan MT (April 2008). "Overexpression of Arabidopsis thaliana tryptophan synthase beta 1 (AtTSB1) in Arabidopsis and tomato confers tolerance to cadmium stress". Plant Cell Environ. 31 (8): 1074–85. doi:10.1111/j.1365-3040.2008.01819.x. PMID 18419734.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Eckert SC, Kubler E, Hoffmann B, Braus GH (June 2000). "The tryptophan synthase-encoding trpB gene of Aspergillus nidulans is regulated by the cross-pathway control system". Mol Gen Genet. 263 (5): 867–76. doi:10.1007/s004380000250. PMID 10905354. S2CID 22836208.
^Ahmed SA, Miles EW, Davies DR (March 1985). "Crystallization and preliminary X-ray crystallographic data of the tryptophan synthase alpha 2 beta 2 complex from Salmonella typhimurium". The Journal of Biological Chemistry. 260 (6): 3716–3718. doi:10.1016/s0021-9258(19)83682-7. PMID 3882715.
^Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR (November 1988). "Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium". The Journal of Biological Chemistry. 263 (33): 17857–17871. doi:10.1016/s0021-9258(19)77913-7. PMID 3053720.
^Raboni S, Bettati S, Mozzarelli A (April 2009). "Tryptophan synthase: a mine for enzymologists". Cell Mol Life Sci. 66 (14): 2391–403. doi:10.1007/s00018-009-0028-0. hdl:11381/2293687. PMID 19387555. S2CID 30220030.
^Fatmi MQ, Ai R, Chang CA (September 2009). "Synergistic regulation and ligand-induced conformational changes of tryptophan synthase". Biochemistry. 48 (41): 9921–31. doi:10.1021/bi901358j. PMID 19764814.
and 25 Related for: Tryptophan synthase information
Tryptophansynthase or tryptophan synthetase is an enzyme (EC 4.2.1.20) that catalyzes the final two steps in the biosynthesis of tryptophan. It is commonly...
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid...
It is an intermediate in the biosynthesis of tryptophan, where it stays inside the tryptophansynthase molecule between the removal of 3-phospho-glyceraldehyde...
on the structure and function of enzymes, especially her work on tryptophansynthase. Miles received her B.A. from the University of Texas at Austin in...
that it wants to repress. Tryptophan biosynthesis involves conversion of chorismate to anthranilate using anthranilate synthase. This enzyme requires either...
Utani and his coworkers substituted 19 amino acids at Trp49 of the tryptophansynthase and he measured the free energy of unfolding. They found that the...
(tryptophan, phenylalanine, and tyrosine). This pathway is not found in mammals. The seven enzymes involved in the shikimate pathway are DAHP synthase...
Dunn MF, Niks D, Ngo H, Barends TR, Schlichting I (June 2008). "Tryptophansynthase: the workings of a channeling nanomachine". Trends in Biochemical...
bacteria. The operon is regulated so that, when tryptophan is present in the environment, the genes for tryptophan synthesis are repressed. The trp operon contains...
in an enzyme active site: the indoline quinonoid intermediate in tryptophansynthase". Journal of the American Chemical Society. 133 (1): 4–7. doi:10...
by glyphosate. EPSP synthase participates in the biosynthesis of the aromatic amino acids phenylalanine, tyrosine, and tryptophan via the shikimate pathway...
aminodeoxychorismate synthase may have evolved from anthranilate synthase (TrpE) - an enzyme that catalyses the production of an intermediate on the path to tryptophan. Enzymes...
Anthranilate synthase creates anthranilate, an important intermediate in the biosynthesis of indole, and by extension, the amino acid tryptophan. Tryptophan can...
Mycobacterium tuberculosis through allosteric inhibition of its tryptophansynthase. High throughput screens further uncovered compounds that inhibit...
hydroxylases. Tetrahydrobiopterin is a cofactor for tryptophan hydroxylase (TPH) for the conversion of L-tryptophan (TRP) to 5-hydroxytryptophan (5-HTP). Phenylalanine...
This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis. Chorismate synthase catalyzes the last of the seven steps in the shikimate...
March 2023. Yanofsky, C (February 2005). "The favorable features of tryptophansynthase for proving Beadle and Tatum's one gene-one enzyme hypothesis". Genetics...
aromatic ring. Among the 20 standard amino acids, histidine, phenylalanine, tryptophan, tyrosine, are classified as aromatic. Aromatic amino acids, excepting...
PMID 17601995 Yanofsky, Charles (2005), "The Favorable Features of TryptophanSynthase for Proving Beadle and Tatum's One Gene–One Enzyme Hypothesis", Genetics...
for: The aromatic amino acids phenylalanine, tryptophan, and tyrosine Indole, indole derivatives and tryptophan 2,3-Dihydroxybenzoic acid (DHB) used for enterobactin...
interacts with the alpha-subunit of tryptophan (TSA) synthase to yield indole. The beta-subunit of tryptophansynthase (TSB) catalyzes condensation of indole...
Global Information