| EC |
4.4.1.43 |
| Accepted name: |
canavanine-γ-lyase |
| Reaction: |
L-canavanine + H2O = L-homoserine + N-hydroxyguanidine (overall reaction)
(1a) L-canavanine = vinylglycine + N-hydroxyguanidine
(1b) vinylglycine = (2E)-2-aminobut-2-enoate (spontaneous)
(1c) (2E)-2-aminobut-2-enoate + H2O = L-homoserine (spontaneous) |
| Other name(s): |
CangL |
| Systematic name: |
L-canavanine N-hydroxyguanidine-lyase (L-homoserine-forming) |
| Comments: |
A pyridoxal 5′-phosphate protein. The enzyme, characterized from the bacterium Pseudomonas canavaninivorans, cleaves a carbon-oxygen bond, releasing N-hydroxyguanidine and an unstable enamine product that tautomerizes to an imine form, which is attacked by a water molecule to form L-homoserine. |
| References: |
| 1. |
Hauth, F., Buck, H., Stanoppi, M. and Hartig, J.S. Canavanine utilization via homoserine and hydroxyguanidine by a PLP-dependent γ-lyase in Pseudomonadaceae and Rhizobiales. RSC Chem. Biol. 3 (2022) 1240–1250. [PMID: 36320885] |
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| [EC 4.4.1.43 created 2022] |
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