The environments of Trp-248 and Trp-330 in tryptophan indole-lyase from Escherichia coli.

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 Lett

journal_title

FEBS letters

authors

Phillips RS,Gollnick P

doi

10.1016/0014-5793(90)81011-c

subject

Has Abstract

pub_date

1990-07-30 00:00:00

pages

213-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(90)81011-C

journal_volume

268

pub_type

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