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mimosinase |
Description |
Mimosine ammonia-lyase (4.3.1.-) |
Catalyzed reaction |
mimosine + H(2)O = 3-hydroxy-4-pyridone + pyruvate + NH(3) |
Cofactor |
Pyridoxal-phosphate. |
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MidD has sequence similarities with aminotransferases, it is not an aminotransferase because it does not require a keto acid as the co-substrate in the degradation reaction. It is a pyridoxal-5'-phosphate (PLP)-dependent enzyme. The catalytic activity of MidD was found to be specific to mimosine. In addition to 3H4P, we also identified pyruvate and ammonia as other degradation products in equimolar quantities of the substrate used. The degradation of mimosine into a ring compound, 3H4P with the release of ammonia indicates that MidD of Rhizobium sp. strain TAL1145 is a CN lyase. |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) mimosinase
BRENDA (activities) mimosinase
KEGG (pathways) mimosinase
PLPMDB (PLP mutants) mimosinase
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References |
Oogai S, Fukuta M, Watanabe K, Inafuku M, Oku H (2019) Molecular characterization of mimosinase and cystathionine β-lyase in the Mimosoideae subfamily member Mimosa pudica J Plant Res 132 667-680. Negi VS, Bingham JP, Li QX, Borthakur D. (2014) A carbon-nitrogen lyase from Leucaena leucocephala catalyzes the first step of mimosine degradation. Plant Physiology 164 922-34. Negi VS , Bingham JP , Li QX , Borthakur D . (2013) midD-encoded 'rhizomimosinase' from Rhizobium sp. strain TAL1145 is a C-N lyase that catabolizes L-mimosine into 3-hydroxy-4-pyridone, pyruvate and ammonia. Amino Acids. 44 1537-47. Articles on mimosinase |
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last changed |
2018/03/23 14:24 |
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