| EC |
4.4.1.2 |
| Accepted name: |
homocysteine desulfhydrase |
| Reaction: |
L-homocysteine + H2O = hydrogen sulfide + NH3 + 2-oxobutanoate (overall reaction)
(1a) L-homocysteine = hydrogen sulfide + 2-aminobut-2-enoate
(1b) 2-aminobut-2-enoate = 2-iminobutanoate (spontaneous)
(1c) 2-iminobutanoate + H2O = 2-oxobutanoate + NH3 (spontaneous) |
| Other name(s): |
homocysteine desulfurase; L-homocysteine hydrogen-sulfide-lyase (deaminating) |
| Systematic name: |
L-homocysteine hydrogen-sulfide-lyase (deaminating; 2-oxobutanoate-forming) |
| Comments: |
A pyridoxal-phosphate protein. 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 catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase |
| References: |
| 1. |
Kallio, R.E. Function of pyridoxal phosphate in desulfhydrase systems of Proteus morganii. J. Biol. Chem. 192 (1951) 371–377. [PMID: 14917685] |
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| [EC 4.4.1.2 created 1961] |
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