Abstract:
:The two tryptophan residues, Trp-248 and Trp-330, in tryptophan indole-lyase (tryptophanase) from E. coli have been separately mutated to phenylalanine using site-directed mutagenesis. Both single tryptophan mutant enzymes have full catalytic activity, but exhibit different fluorescence and near-UV circular dichroism spectra. These results indicate that Trp-330 is more deeply buried than is Trp-248, and is in a more asymmetric environment. Neither residue reacts with N-bromosuccinimide (NBS), although tryptophan indole-lyase is inactivated by NBS. These results demonstrate that the tryptophan residues in tryptophan indole-lyase are not catalytically essential.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Phillips RS,Gollnick Pdoi
10.1016/0014-5793(90)81011-csubject
Has Abstractpub_date
1990-07-30 00:00:00pages
213-6issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(90)81011-Cjournal_volume
268pub_type
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