KEGG   ENZYME: 4.3.3.8
Entry
EC 4.3.3.8                  Enzyme                                 
Name
mimosinase;
mimosine amidohydrolase (incorrect)
Class
Lyases;
Carbon-nitrogen lyases;
Amine-lyases
Sysname
(2S)-2-amino-3-[3-hydroxy-4-oxopyridin-1(4H)-yl]propanoate 3-hydroxy-4H-pyrid-4-one-lyase (2-aminoprop-2-enoate-forming)
Reaction(IUBMB)
L-mimosine + H2O = 3-hydroxy-4H-pyrid-4-one + pyruvate + NH3 (overall reaction) [RN:R04350];
(1a) L-mimosine = 3-hydroxy-4H-pyrid-4-one + 2-aminoprop-2-enoate [RN:R13116];
(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)  [RN:R11099];
(1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) [RN:R11100]
Reaction(KEGG)
Substrate
L-mimosine [CPD:C04771];
H2O [CPD:C00001];
2-aminoprop-2-enoate [CPD:C02218];
2-iminopropanoate [CPD:C20904]
Product
3-hydroxy-4H-pyrid-4-one [CPD:C03927];
pyruvate [CPD:C00022];
NH3 [CPD:C00014];
2-aminoprop-2-enoate [CPD:C02218];
2-iminopropanoate [CPD:C20904]
Comment
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.
History
EC 4.3.3.8 created 1989 as EC 3.5.1.61, transferred 2022 to EC 4.3.3.8
Orthology
K08079  mimosinase
K26364  mimosinase
Genes
PCIN129286560 129309431 129309784 129310132
MAZANFX31_05755
MSUWGCM10025863_27360
MINVT9R20_01880
MESTPTQ19_14765
MHUMNNL39_06090
MDBOVN18_05945
AGROJSQ78_03085
NAEIGCM126_08210
BSPOL1F31_06095
DSSGCM25873_13700
BROObrsh051_11580
ACTYOG774_08480
AWLP8A24_03490
ACASP7079_02975
TBERQPC17_05760
AUUCJ184_005965
ATIMCYJ17_0006095
AMASQU670_06405
ACAPMANAM107_19980
AUOR3I39_06790
GEUCJ185_002670
GHMCJ187_004740
VCBCYK25_004045
MICAP0L94_01000
 » show all
Reference
1
  Authors
Tangendjaja, B., Lowry, J.B. and Wills, R.H.
  Title
Isolation of a mimosine degrading enzyme from Leucaena leaf.
  Journal
J Sci Food Agric 37:523-526 (1986)
Reference
2  [PMID:24351687]
  Authors
Negi VS, Bingham JP, Li QX, Borthakur D.
  Title
A carbon-nitrogen lyase from Leucaena leucocephala catalyzes the first step of mimosine degradation.
  Journal
Plant Physiol 164:922-34 (2014)
DOI:10.1104/pp.113.230870
Reference
3  [PMID:31368041]
  Authors
Oogai S, Fukuta M, Watanabe K, Inafuku M, Oku H.
  Title
Molecular characterization of mimosinase and cystathionine beta-lyase in the Mimosoideae subfamily member Mimosa pudica.
  Journal
J Plant Res 132:667-680 (2019)
DOI:10.1007/s10265-019-01128-4
  Sequence
Reference
4  [PMID:35908235]
  Authors
Oogai S, Fukuta M, Inafuku M, Oku H.
  Title
Isolation and characterization of mimosine degrading enzyme from Arthrobacter sp. Ryudai-S1.
  Journal
World J Microbiol Biotechnol 38:172 (2022)
DOI:10.1007/s11274-022-03344-y
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.3.3.8
IUBMB Enzyme Nomenclature: 4.3.3.8
ExPASy - ENZYME nomenclature database: 4.3.3.8
BRENDA, the Enzyme Database: 4.3.3.8
CAS: 104118-49-2

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