CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family

Enzyme Information

4.4.1.1
Cystathionine gamma-lyase.
based on mapping to UniProt P32929
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)

P32929
CGL_HUMAN
Homo sapiens
Cystathionine gamma-lyase

PDB Structure

PDB 2NMP
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S
Sun, Q., Collins, R., Huang, S., Holmberg-Schiavone, L., Anand, G.S., Tan, C.-H., van-den-Berg, S., Deng, L.-W., Moore, P.K., Karlberg, T., Sivaraman, J.
J.Biol.Chem.