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 1UKJ
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Detailed structure of L-Methionine -Lyase from Pseudomonas putida
Misaki, S., Takimoto, A., Takakura, T., Yoshioka, T., Yamashita, M., Tamura, T., Tanaka, H., Inagaki, K.
To be Published