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| EC | 4.4.1.11 | ||
| Accepted name: | methionine γ-lyase | ||
| Reaction: | L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate (overall reaction) (1a) L-methionine = methanethiol + 2-aminobut-2-enoate (1b) 2-aminobut-2-enoate = 2-iminobutanoate (spontaneous) (1c) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (spontaneous) |
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| For diagram of reaction mechanism, click here | |||
| Other name(s): | L-methioninase; methionine lyase; methioninase; methionine dethiomethylase; L-methionine γ-lyase; L-methionine methanethiol-lyase (deaminating) | ||
| Systematic name: | L-methionine methanethiol-lyase (deaminating; 2-oxobutanoate-forming) | ||
| Comments: | A pyridoxal-phosphate protein. 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 catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme is involved in L-methionine catabolism. | ||
| Links to other databases: | BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 42616-25-1 | ||
| References: |
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