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Information on EC 4.2.1.20 - tryptophan synthase and Organism(s) Thermus thermophilus and UniProt Accession P16608

for references in articles please use BRENDA:EC4.2.1.20
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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.20 tryptophan synthase
IUBMB Comments
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
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Thermus thermophilus
UNIPROT: P16608 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trps, tryptophan synthase, tryptophan synthetase, tsase, alphats, trpb2, tryptophan synthase beta, trp synthase, trpb1, beta subunit of tryptophan synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
indoleglycerol phosphate aldolase
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L-tryptophan synthetase
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synthase, tryptophan
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-
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tryptophan desmolase
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tryptophan synthetase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addition
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-serine hydro-lyase [adding 1-C-(indol-3-yl)glycerol 3-phosphate; L-tryptophan and glyceraldehyde-3-phosphate-forming]
A pyridoxal-phosphate protein. The alpha-subunit catalyses the conversion of 1-C-(indol-3-yl)glycerol 3-phosphate to indole and D-glyceraldehyde 3-phosphate (this reaction was included formerly under EC 4.1.2.8). The indole migrates to the beta-subunit where, in the presence of pyridoxal 5'-phosphate, it is combined with L-serine to form L-tryptophan. In some organisms this enzyme is part of a multifunctional protein that also includes one or more of the enzymes EC 2.4.2.18 (anthranilate phosphoribosyltransferase), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.1.3.27 (anthranilate synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase). In thermophilic organisms, where the high temperature enhances diffusion and causes the loss of indole, a protein similar to the beta subunit can be found (EC 4.2.1.122). That enzyme cannot combine with the alpha unit of EC 4.2.1.20 to form a complex.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-52-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
HB8
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A7R7TE40_THETH
404
0
43809
TrEMBL
-
A0A3P4ANZ5_THETH
404
0
43830
TrEMBL
-
A0A510HTE1_THETH
404
0
43812
TrEMBL
-
A0A1J1EEZ5_THETH
405
0
44007
TrEMBL
-
A0A8D6LJH1_THETH
265
0
28311
TrEMBL
-
A0A7R7TDN2_THETH
271
0
28947
TrEMBL
-
A0A3P4AQD1_THETH
265
0
28390
TrEMBL
-
A0A1J1EQL5_THETH
265
0
28449
TrEMBL
-
A0A510HR87_THETH
265
0
28331
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of alpha-subunit of tryptophan synthase, oil batch method, discussion of the thermostabilization mechanism of the tryptophan synthase alpha-subunit on the basis of crystal structures and DSC data of the alpha-subunit orthologs from mesophilic, extreme thermophilic, and hyperthermophilic organisms
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Asada, Y.; Sawano, M.; Ogasahara, K.; Nakamura, J.; Ota, M.; Kuroishi, C.; Sugahara, M.; Yutani, K.; Kunishima, N.
Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry
J. Biochem.
138
343-353
2005
Thermus thermophilus (Q5SJC0), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SJC0)
Manually annotated by BRENDA team