CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate Aminotransferase, domain 1
Functional Family

Enzyme Information

4.4.1.2
Homocysteine desulfhydrase.
based on mapping to UniProt P13254
L-homocysteine + H(2)O = H(2)S + NH(3) + 2-oxobutanoate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing hydrogen sulfide 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.
4.4.1.11
Methionine gamma-lyase.
based on mapping to UniProt P13254
L-methionine + H(2)O = methanethiol + NH(3) + 2-oxobutanoate.
-!- The enzyme cleaves a carbon-sulfur bond, releasing methanethiol 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. -!- The enzyme is involved in L-methionine catabolism.

UniProtKB Entries (1)

P13254
MEGL_PSEPU
Pseudomonas putida
L-methionine gamma-lyase

PDB Structure

PDB 3VK2
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The role of amino acid residues in the active site of L-methionine gamma-lyase from Pseudomonas putida.
Fukumoto, M., Kudou, D., Murano, S., Shiba, T., Sato, D., Tamura, T., Harada, S., Inagaki, K.
Biosci.Biotechnol.Biochem.