70082-70-1Relevant articles and documents
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Skarabal et al.
, p. 995,997 (1979)
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L-Tryptophan 2',3'-oxidase from Chromobacterium violaceum catalyzes the synthesis of &α,&β-dehydrotryptophanyl residues in peptides and proteins: A tool for chemical modification and labelling of peptides and proteins
Genet, R,Denoyelle, C,Menez, A
, p. 848 - 850 (2007/10/02)
In 1975, Davis et al. reported the capacity of Chromobacterium violaceum (ATCC 12472) to transform Cbz-L-tryptophan into its α,β-dehydro derivative.However, reaction specificity and structural features of the putative enzyme which is responsible for this activity were not determined.We have isolated from this strain an enzyme designated L-tryptophan 2',3'-oxidase, which catalyzes the formation of a double bond at the Cα-Cβ position of tryptophan residues.Using a variety of tryptophan derivatives, we have demonstrated thatthe enzyme is highly specific for unsubstituted indole containing compounds and showed that the enzyme not only acts on isolated tryptophanyl side-chains but is also capable of dehydrogenating tryptophan residues in peptides and proteins.
