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Information on EC 4.3.3.8 - mimosinase
for references in articles please use BRENDA:EC4.3.3.8
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IUBMB Comments
A pyridoxal 5′-phosphate protein. The enzyme degrades the toxic amino acid L-mimosine. It cleaves a carbon-nitrogen bond, releasing 3-hydroxy-4H-pyrid-4-one and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. It is thought to have evolved from EC 4.4.1.13, cysteine-S-conjugate β-lyase. It has been described in both mimosine-producing plants and some bacteria.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
showSynonyms
EC 3.5.1.61, mimosine amidohydrolase, mimosine degrading enzyme, mimosine-degrading enzyme, Mp mimosinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.5.1.61
-
-
formerly
-
mimosine amidohydrolase
-
-
incorrect
-
mimosine degrading enzyme
-
-
-
-
mimosine-degrading enzyme
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
(1b)
-
-
-
2-iminopropanoate + H2O = pyruvate + ammonia
(1c)
-
-
-
L-mimosine + H2O = 3-hydroxy-4H-pyrid-4-one + pyruvate + ammonia
overall reaction
-
-
-
L-mimosine = 3-hydroxy-4H-pyrid-4-one + 2-aminoprop-2-enoate
(1a)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of linear amides
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(2S)-2-amino-3-[3-hydroxy-4-oxopyridin-1(4H)-yl]propanoate 3-hydroxy-4H-pyrid-4-one-lyase (2-aminoprop-2-enoate-forming)
A pyridoxal 5'-phosphate protein. The enzyme degrades the toxic amino acid L-mimosine. It cleaves a carbon-nitrogen bond, releasing 3-hydroxy-4H-pyrid-4-one and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. It is thought to have evolved from EC 4.4.1.13, cysteine-S-conjugate beta-lyase. It has been described in both mimosine-producing plants and some bacteria.
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CAS REGISTRY NUMBER
COMMENTARY
104118-49-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4(1H)-pyrid-4-one + L-serine
-
Substrates: 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
Products: DHP, less toxic than mimosine
Products: DHP, less toxic than mimosine
?
(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
?
-
Substrates: -
Products: -
Products: -
?
cystathionine + H2O
homocysteine + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
Substrates: 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
Products: product identification by by electrospray ionization-tandem mass spectrometry
Products: product identification by by electrospray ionization-tandem mass spectrometry
?
mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: cystathionine
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O
3-hydroxy-4H-pyrid-4-one + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
cystathionine + H2O
homocysteine + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
mimosine + H2O
3-hydroxy-4-(1H)-pyridone + pyruvate + NH3
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydroxylamine
complete inhibition at 0.05 mM, reversible by 100 nM pyridoxal 5'-phosphate
tyrosine
-
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
-
3-hydroxy-4(1H)-pyridone, DHP, 0.4-3.2 mM, no effect, no feedback inhibitor
-
additional information
no competitive inhibition by L-tyrosine, L-phenylalanine, and L-tryptophan
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.64
beta-[N-(3-hydroxy-4(1H)-pyridone)]-alpha-aminopropionic acid
-
mimosine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 12
high catalytic activities at pH 7.5-10.0, inactive below pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22 - 45
enzyme catalytic activity sharply decreases at 45°C or higher and below 22°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
collected from University of Hawaii research station, Waimanalo, Honolulu
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the enzyme has a chloroplast transit peptide
brenda
the enzyme sequence contains a chloroplast transit peptide
brenda
additional information
the enzyme sequence contains a 43 amino acid signal peptide
-
brenda
additional information
the enzyme sequence contains a signal peptide
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
physiological function
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
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
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
physiological function
the strain is able to degrade and assimilate mimosine as a nitrogen and carbon source
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). F1T2J8_9MICC
388
0
43025
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and docking of mimosine. 11 amino acid residues are strongly interacting with mimosine-PLP
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y263L
contrary to wild-type, mutant also accepts cystathionine as substrate
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
purified recombinant enzyme, pH 8.5, 37°C, around 80% activity remaining, fairly stable up to 40°C
50
70
50
purified recombinant enzyme, pH 8.5, 37°C, the enzyme activity shows a sharp reduction
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification from sonic extract, using stepwise ammonium precipitation, DEAE-Sephadex A-25 ion-exchange chromatography and native PAGE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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)
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)
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)
brenda
Oogai, S.; Fukuta, M.; Inafuku, M.; Oku, H.
Isolation and characterization of mimosine degrading enzyme from Arthrobacter sp. Ryudai-S1
World J. Microbiol. Biotechnol.
38
172
2022
Arthrobacter sp. Ryudai-S1 (F1T2J8)
brenda
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