We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00667Beta-eliminating lyases pyridoxal-phosphate attachment site
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00667
Description
Tryptophan indole-lyase (EC 4.1.99.1) (tryptophanase) and tyrosine phenol-lyase (EC 4.1.99.2) (β-tyrosinase) are related pyridoxal-phosphate dependent homotetrameric enzymes [1]. Tryptophan indole-lyase catalyzes the transformation of tryptophan into indole, pyruvate and ammonia and tyrosine phenol-lyase transforms tyrosine into phenol, pyruvate and ammonia.
Both enzymes are proteins that contains 450 to 470 amino acids. The pyridoxal-phosphate group is attached to a lysine residue in the central section of the sequence.
Last update:December 2004 / Pattern and text revised.
-------------------------------------------------------------------------------
Technical section
PROSITE method (with tools and information) covered by this documentation:
Reference
| 1 | Authors | Iwamori S. Yoshino S. Ishiwata K. Makiguchi N. |
| Source | J. Ferment. Bioeng. 72:147-151(1991). |
Copyright
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.