CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Cystathionine gamma-synthase homolog

Enzyme Information

4.4.1.13
Cysteine-S-conjugate beta-lyase.
based on mapping to UniProt P53780
An L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate.
-!- A pyridoxal 5'-phosphate protein. -!- The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions. -!- The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases. -!- Formerly EC 4.4.1.6 and EC 4.4.1.8.

UniProtKB Entries (1)

P53780
METC_ARATH
Arabidopsis thaliana
Cystathionine beta-lyase, chloroplastic

PDB Structure

PDB 1IBJ
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity
Breitinger, U., Clausen, T., Ehlert, S., Huber, R., Laber, B., Schmidt, F., Pohl, E., Messerschmidt, A.
Plant Physiol.