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EC Tree
IUBMB Comments An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mimosinase, mp mimosinase, mimosine amidohydrolase,
more
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mimosine degrading enzyme
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mimosine-degrading enzyme
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O = 3-hydroxy-4H-pyrid-4-one + L-serine
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hydrolysis of linear amides
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mimosine amidohydrolase
An enzyme from Leucaena leucocephala leaf, which also contains the toxic amino acid, mimosine.
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4(1H)-pyrid-4-one + L-serine
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
beta-[N-(3-hydroxy-4(1H)-pyridone)]-alpha-aminopropionic acid + H2O
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cystathionine + H2O
homocysteine + pyruvate + NH3
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mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
additional information
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4(1H)-pyrid-4-one + L-serine
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free toxic amino acid mimosine, 3-(3-hydroxy-4-oxo-1(4H)-pyridyl)-L-alanine, beta-[N-(3-hydroxy-4(1H)-pyridone)]-alpha-aminopropionic acid, beta-[N-(3-hydroxy-4-oxypyridyl)]-alpha-aminopropionic acid
DHP, less toxic than mimosine
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4(1H)-pyrid-4-one + L-serine
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free toxic amino acid mimosine, 3-(3-hydroxy-4-oxo-1(4H)-pyridyl)-L-alanine, beta-[N-(3-hydroxy-4(1H)-pyridone)]-alpha-aminopropionic acid, beta-[N-(3-hydroxy-4-oxypyridyl)]-alpha-aminopropionic acid
DHP, less toxic than mimosine
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
i.e. mimosine, a toxic nonprotein aromatic amino acid. Dependence of the enzyme on pyridoxal 5'-phosphate and the production of 3-hydroxy-4H-pyrid-4-one with the release of ammonia indicate that the enzyme is a carbon-nitrogen lyase
product identification by by electrospray ionization-tandem mass spectrometry
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mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
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mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
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additional information
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substrate docking study. Cystathionine is a larger molecule than mimosine and consists of propyl (C3) and ethyl (C2) chains bound by a thioether linkage. The ethyl chain moiety and PLP of the complex interacts with Arg417, Lys255, Arg105', and Gly133 as is the case for mimosine
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additional information
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substrate docking study. Cystathionine is a larger molecule than mimosine and consists of propyl (C3) and ethyl (C2) chains bound by a thioether linkage. The ethyl chain moiety and PLP of the complex interacts with Arg417, Lys255, Arg105', and Gly133 as is the case for mimosine
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(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
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cystathionine + H2O
homocysteine + pyruvate + NH3
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mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
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mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
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pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
dependent on, enzyme-bound
additional information
no requirement for an 2oxo acid
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additional information
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no requirement for an 2oxo acid
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hydroxylamine
complete inhibition at 0.05 mM, reversible by 100 nM pyridoxal 5'-phosphate
L-Phe
competitive inhibition
L-Trp
competitive inhibition
L-Tyr
competitive inhibition
tyrosine
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competitive inhibitor, 0.14 mM: 90% of maximal activity, 0.28 mM: 80% of maximal activity, 0.42 mM: 78% of maximal activity, 0.56 mM: 72% of maximal activity, 0.96 mM: 56% of maximal activity, 1 mM: 50% of maximal activity
additional information
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3-hydroxy-4(1H)-pyridone, DHP, 0.4-3.2 mM, no effect, no feedback inhibitor
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additional information
no competitive inhibition by L-tyrosine, L-phenylalanine, and L-tryptophan
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additional information
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no competitive inhibition by L-tyrosine, L-phenylalanine, and L-tryptophan
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1.64
beta-[N-(3-hydroxy-4(1H)-pyridone)]-alpha-aminopropionic acid
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mimosine
0.05
cystathionine
pH 8.5, 37°C, recombinant enzyme
1.95
mimosine
pH 8.5, 37°C, recombinant enzyme
additional information
additional information
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reaction kinetics
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310
cystathionine
pH 8.5, 37°C, recombinant enzyme
12180
mimosine
pH 8.5, 37°C, recombinant enzyme
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6200
cystathionine
pH 8.5, 37°C, recombinant enzyme
6246
mimosine
pH 8.5, 37°C, recombinant enzyme
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7 - 12
high catalytic activities at pH 7.5-10.0, inactive below pH 7.0
additional information
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37
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22 - 45
enzyme catalytic activity sharply decreases at 45°C or higher and below 22°C
35 - 65
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appreciable activity between
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UniProt
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(Lam) de Wit cv. Cunningham
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collected from University of Hawaii research station, Waimanalo, Honolulu
UniProt
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gene seq3
UniProt
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tropical legume
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mature
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the enzyme has a chloroplast transit peptide
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the enzyme sequence contains a chloroplast transit peptide
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additional information
the enzyme sequence contains a 43 amino acid signal peptide
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additional information
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the enzyme sequence contains a 43 amino acid signal peptide
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additional information
the enzyme sequence contains a signal peptide
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additional information
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the enzyme sequence contains a signal peptide
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malfunction
mutational analysis of Mp mimosinase reveals that the disruption of a disulfide bond in the vicinity of the pyridoxal 5'-phosphate domain increases the enzyme's preference toward cystathionine
physiological function
mimosinase is an important enzyme especially in the context of metabolic engineering of plant secondary metabolite as it catalyzes the degradation of mimosine, which is a toxic secondary metabolite found in all Leucaena and Mimosa species
metabolism
the carbon-nitrogen lyase catalyzes the first step of mimosine degradation. Mimosine is a toxic nonprotein aromatic amino acid
metabolism
molecular relationship between mimosinase and cystathionine beta-lyase (CBL, UniProt ID A0A0M3VI47, EC 4.4.1.13). The recombinant Mp mimosinase degrades both mimosine and cystathionine with a much higher turnover number for mimosine compared with cystathionine, and Mp CBL utilizes only cystathionine as a substrate
additional information
homology modeling and molecular dynamics simulations of Mp mimosinase suggest a closer coordination of the residues that interact with mimosine at the active site compared with cystathionine, indicating a more compact pocket size for mimosine degradation, substrate docking study. Active site structure
additional information
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homology modeling and molecular dynamics simulations of Mp mimosinase suggest a closer coordination of the residues that interact with mimosine at the active site compared with cystathionine, indicating a more compact pocket size for mimosine degradation, substrate docking study. Active site structure
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F1T2J8_9MICC
388
0
43025
TrEMBL
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A8CEI3_LEULE
443
0
48338
TrEMBL
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U6BYK3_MIMPU
442
0
48092
TrEMBL
Secretory Pathway (Reliability: 5 )
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45000
x * 45000 recombinant enzyme, SDS-PAGE
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x * 45000 recombinant enzyme, SDS-PAGE
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40
purified recombinant enzyme, pH 8.5, 37°C, around 80% activity remaining, fairly stable up to 40°C
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purified recombinant enzyme, pH 8.5, 37°C, the enzyme activity shows a sharp reduction
70
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partial denaturation of the enzyme at
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purified recombinant GST-tagged enzyme, pH 8.0, stable up to
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recombinant enzyme from Escherichia coli
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene seq3, DNA and amino acid sequence determination and analysis, codon optimization and recombinant expression in Escherichia coli
generation of a synthetic gene, cloning method overview, subcloning in Escherichia coli strain JM109, sequence comparison with wild-type gene, recombinant enzyme expression of the synthetic gene syn-mimosinase ORF in Escherichia coli strain BL21(DE3) pLysS
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nutrition
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implication for reducing the toxicity of Leucaena used for stock feed, the product 3-hydroxy-4(1H)-pyrid-4-one, DHP, is goitrogenic in animals but is less toxic than mimosine, conversion of mimosine to DHP is therefore beneficial for the use of Leucaena as animal feed
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Tangendjaja, B.; Lowry, J.B.; Wills, R.B.H.
Isolation of a mimosine degrading enzyme from Leucaena leaf
J. Sci. Food Agric.
37
523-526
1986
Leucaena leucocephala
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brenda
Tangendjaja, B.; Lowry, J.B.; Wills, R.B.H.
Optimisation of conditions for the degradation of mimosine in Leucaena leucocephala leaf
J. Sci. Food Agric.
35
613-616
1984
Leucaena leucocephala
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brenda
Negi, V.S.; Bingham, J.P.; Li, Q.X.; Borthakur, D.
A carbon-nitrogen lyase from Leucaena leucocephala catalyzes the first step of mimosine degradation
Plant Physiol.
164
922-934
2014
Leucaena leucocephala (A8CEI3), Leucaena leucocephala
brenda
Oogai, S.; Fukuta, M.; Watanabe, K.; Inafuku, M.; Oku, H.
Molecular characterization of mimosinase and cystathionine beta-lyase in the Mimosoideae subfamily member Mimosa pudica
J. Plant Res.
132
667-680
2019
Mimosa pudica (U6BYK3), Mimosa pudica
brenda
Negi, V.S.; Borthakur, D.
Heterologous expression and characterization of mimosinase from Leucaena leucocephala
Methods Mol. Biol.
1405
59-77
2016
Leucaena leucocephala (A8CEI3), Leucaena leucocephala
brenda
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