ID   4.4.1.13
DE   cysteine-S-conjugate beta-lyase.
AN   alkylcysteine lyase.
AN   alkyl cysteine lyase.
AN   cystathionine beta-lyase.
AN   cystine lyase.
AN   L-cysteine-S-conjugate thiol-lyase (deaminating).
AN   S-alkylcysteinase.
AN   S-alkylcysteine lyase.
AN   S-alkyl-L-cysteine lyase.
AN   S-alkyl-L-cysteine sulfoxide lyase.
CA   an S-substituted L-cysteine + H2O = a thiol + pyruvate + NH4(+).
CC   -!- A pyridoxal 5'-phosphate protein.
CC   -!- The enzyme is promiscuous regarding the moiety conjugated to
CC       L-cysteine, and can accept both aliphatic and aromatic substitutions.
CC   -!- The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an
CC       unstable enamine product that tautomerizes to an imine form, which
CC       undergoes a hydrolytic deamination to form pyruvate and ammonia.
CC   -!- While bacteria and plants have dedicated enzymes, all of the animal
CC       enzymes discovered thus far are bifunctional, most of which also act
CC       as aminotransferases.
CC   -!- Formerly EC 4.4.1.6 and EC 4.4.1.8.
DR   Q08432, CBL_BACSU  ;  Q93QC6, CBL_CORGT  ;  Q64HC5, CBL_CORST  ;
DR   A0A0M3VI47, CBL_MIMPU  ;  P63503, CBL_MYCBO  ;  Q9CBM9, CBL_MYCLE  ;
DR   P9WQ82, CBL_MYCTO  ;  P9WQ83, CBL_MYCTU  ;  Q1K8G0, CBL_NEUCR  ;
DR   O94350, CBL_SCHPO  ;  Q5SHW0, CBL_THET8  ;  Q16773, KAT1_HUMAN ;
DR   Q8BTY1, KAT1_MOUSE ;  Q08415, KAT1_RAT   ;  Q0P5G4, KAT3_BOVIN ;
DR   Q7T3E5, KAT3_DANRE ;  Q6YP21, KAT3_HUMAN ;  Q71RI9, KAT3_MOUSE ;
DR   Q58FK9, KAT3_RAT   ;  Q54KM6, KAT_DICDI  ;  P23256, MALY_ECOLI ;
DR   P53780, METC_ARATH ;  O31632, METC_BACSU ;  Q07703, METC_BORAV ;
DR   Q83A83, METC_COXBU ;  P06721, METC_ECOLI ;  P44527, METC_HAEIN ;
DR   P0A4K2, METC_LACLA ;  P0C2T9, METC_LACLC ;  A2RM21, METC_LACLM ;
DR   P85217, METC_PAPLA ;  Q52811, METC_RHIJ3 ;  P18949, METC_SALTY ;
DR   Q4L332, METC_STAHJ ;  P43623, METC_YEAST ;  U6BYK3, MIMOS_MIMPU;
DR   P53101, STR3_YEAST ;
//