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Parent Class: | EC-Numbers → 4 -- Lyases → 4.2 -- Carbon-oxygen lyases → 4.2.1 -- Hydro-lyases |
Synonyms: tryptophan synthase β2
Systematic Name: L-serine hydro-lyase [adding indole, L-tryptophan-forming]
Unification Links: BRENDA:4.2.1.122, ENZYME:4.2.1.122, IUBMB-ExplorEnz:4.2.1.122
Reaction:
L-serine + indole → L-tryptophan + H2O
Enzymes and Genes:
tryptophan synthase, β subunit dimer:
trpB (
Escherichia coli K-12 substr. MG1655
)
tryptophan synthase:
TSBType2 (
Arabidopsis thaliana col
)
tryptophan synthase, beta subunit:
TSB1 (
Arabidopsis thaliana col
)
tryptophan synthase β subunit dimer:
trpB (
Thermococcus kodakarensis
)
tryptophan synthase β2 dimer:
trpB2 (
Thermotoga maritima
)
tryptophan synthase β1 dimer:
trpB1 (
Thermotoga maritima
)
Summary:
Most mesophilic bacteria have a multimeric tryptophan synthase complex (
EC 4.2.1.20) that forms L-tryptophan from L-serine and 1-C-(indol-3-yl)glycerol 3-phosphate via an indole intermediate. This intermediate, which is formed by the α subunits, is transferred in an internal tunnel to the β units, which convert it to tryptophan. In thermophilic organisms the high temperature enhances diffusion and causes the loss of indole. This enzyme, which does not combine with the α unit to form a complex, salvages the lost indole back to L-tryptophan. It has a much lower Km for indole than the β subunit of
EC 4.2.1.20.
References
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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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