{PDOC00667} {PS00853; BETA_ELIM_LYASE} {BEGIN} *************************************************************** * Beta-eliminating lyases pyridoxal-phosphate attachment site * *************************************************************** Tryptophan indole-lyase (EC 4.1.99.1) (tryptophanase) and tyrosine phenol- lyase (EC 4.1.99.2) (beta-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. -Consensus pattern: [YV]-x-D-x(3)-M-S-[GA]-K-K-D-x-[LIVMF]-[LIVMAG]-x-[LIVM]- G-G [The second K is the pyridoxal-P attachment site] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Iwamori S., Yoshino S., Ishiwata K., Makiguchi N. J. Ferment. Bioeng. 72:147-151(1991). -------------------------------------------------------------------------------- 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 https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}