KEGG ENZYME: 4.3.3.8

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)

R04350 R11099 R11100 R13116

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

PCIN:

129286560 129309431 129309784 129310132

MAZA:

NFX31_05755

MSUW:

GCM10025863_27360

MINV:

T9R20_01880

MEST:

PTQ19_14765

MHUM:

NNL39_06090

MDB:	OVN18_05945

AGRO:

JSQ78_03085

NAEI:

GCM126_08210

BSPO:

L1F31_06095

DSS:	GCM25873_13700

BROO:

brsh051_11580

ACTY:

OG774_08480

AWL:	P8A24_03490

ACAS:

P7079_02975

TBER:

QPC17_05760

AUU:	CJ184_005965

ATIM:

CYJ17_0006095

AMAS:

QU670_06405

ACAP:

MANAM107_19980

AUO:	R3I39_06790

ALIL:

D5R93_08720

GEU:	CJ185_002670

GHM:	CJ187_004740

VCB:	CYK25_004045

PHON:

BH719_02830

MICA:

P0L94_01000

» show all

Reference

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

[ag:BAN57423]

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

[ag:BAK08884]

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

All links

Chemical substance (7)   
   KEGG COMPOUND (7)   
Chemical reaction (7)   
   KEGG REACTION (4)   
   KEGG RCLASS (3)   
Gene (34)   
   KEGG ORTHOLOGY (2)   
   KEGG GENES (32)   
All databases (48)   

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