CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate Aminotransferase, domain 1
Functional Family Cystathionine gamma-synthase

Enzyme Information

4.4.1.1
Cystathionine gamma-lyase.
based on mapping to UniProt P31373
L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also catalyzes the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia. -!- Formerly EC 4.2.1.15.

UniProtKB Entries (1)

P31373
CYS3_YEAST
Saccharomyces cerevisiae S288C
Cystathionine gamma-lyase

PDB Structure

PDB 1N8P
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Determinants of Enzymatic Specificity in the Cys-Met-Metabolism PLP-Dependent Enzymes Family: Crystal Structure of Cystathionine gamma-lyase from Yeast and Intrafamiliar Structural Comparison
Messerschmidt, A., Worbs, M., Steegborn, C., Wahl, M.C., Huber, R., Laber, B., Clausen, T.
BIOL.CHEM.