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EC Tree
IUBMB Comments A pyridoxal 5'-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-thiocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme from Brassica oleracea var. italica (broccoli) does not act on cysteine or cystathionine.
The enzyme appears in viruses and cellular organisms
Synonyms
BOCL3, cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming),
CORI3 ,
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cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming)
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CORI3
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2-aminoprop-2-enoate = 2-iminopropanoate
(1b), spontaneous
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2-iminopropanoate + H2O = pyruvate + NH3
(1c), spontaneous
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L-cystine + H2O = L-thiocysteine + pyruvate + NH3
overall reaction
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L-cystine = L-thiocysteine + 2-aminoprop-2-enoate
(1a)
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L-cystine thiocysteine-lyase (deaminating; pyruvate-forming)
A pyridoxal 5'-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-thiocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme from Brassica oleracea var. italica (broccoli) does not act on cysteine or cystathionine.
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2-aminoprop-2-enoate
2-iminopropanoate
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spontaneous partial reaction
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2-iminopropanoate + H2O
pyruvate + NH3
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spontaneous partial reaction
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L-cysteine S-sulfate + H2O
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L-cystine
L-thiocysteine + 2-aminoprop-2-enoate
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L-cystine + H2O
L-thiocysteine + pyruvate + NH3
L-djenkolic acid + H2O
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18-24% of the activity with L-cystine
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S-ethyl L-cysteine + H2O
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71% of the activity with L-cystine
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S-ethyl L-cysteine sulfoxide + H2O
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S-methyl L-cysteine + H2O
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29% of the activity with L-cystine
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S-methyl L-cysteine sulfoxide + H2O
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S-propyl L-cysteine + H2O
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29% of the activity with L-cystine
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additional information
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L-cystine + H2O
L-thiocysteine + pyruvate + NH3
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L-cystine + H2O
L-thiocysteine + pyruvate + NH3
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L-cystine + H2O
L-thiocysteine + pyruvate + NH3
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overall reaction
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S-ethyl L-cysteine sulfoxide + H2O
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S-ethyl L-cysteine sulfoxide + H2O
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48% of the activity with L-cystine
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S-ethyl L-cysteine sulfoxide + H2O
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64% of the activity with L-cystine
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S-methyl L-cysteine sulfoxide + H2O
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S-methyl L-cysteine sulfoxide + H2O
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37% of the activity with L-cystine
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S-methyl L-cysteine sulfoxide + H2O
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46% of the activity with L-cystine
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additional information
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the enzyme catalyzes beta-elimination of L-cystine to yield thiocysteine, pyruvate and possibly ammonia. S-Methyl L-cysteine sulfoxide and S-ethyl L-cysteine sulfoxide are substrates but are less suitable than L-cystine. No substrates: D-cystine, L- and o-cysteine and cystathionine
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additional information
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negligible activity with L-cystathionine
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2-aminoprop-2-enoate
2-iminopropanoate
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spontaneous partial reaction
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2-iminopropanoate + H2O
pyruvate + NH3
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spontaneous partial reaction
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L-cystine
L-thiocysteine + 2-aminoprop-2-enoate
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L-cystine + H2O
L-thiocysteine + pyruvate + NH3
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overall reaction
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S-ethyl L-cysteine sulfoxide + H2O
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48% of the activity with L-cystine
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S-methyl L-cysteine sulfoxide + H2O
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37% of the activity with L-cystine
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additional information
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the enzyme catalyzes beta-elimination of L-cystine to yield thiocysteine, pyruvate and possibly ammonia. S-Methyl L-cysteine sulfoxide and S-ethyl L-cysteine sulfoxide are substrates but are less suitable than L-cystine. No substrates: D-cystine, L- and o-cysteine and cystathionine
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pyridoxal 5'-phosphate
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carboxymethoxylamine
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0.5 mM, 2% residual activity; 0.5 mM, complete inhibition
cyanide
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12.5 mM, 5% residual activity
DL-homocysteine
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2.5 mM, 59% residual activity
L-cysteine
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linear noncompetitive inhibitor
pyridoxal
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2.5 mM, 63% residual activity
additional information
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not inhibitory at 0.5 mM, iodoacetate, N-ethylmaleimide, EDTA; not inhibitory: iodoacetate, N-ethylmaleimide and EDTA
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hydroxylamine
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12.5 mM, 3% residual activity
hydroxylamine
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0.5 mM, 15% residual activity; 0.5 mM, complete inhibition
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0.0812
L-cystine
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pH 8.4, 30°C
2.32
L-cystine
pH 7.6, 22°C
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1.5
L-cysteine
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pH 8.4, 30°C
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3 - 11
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more than 50% of maximum activity
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UniProt
brenda
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SwissProt
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brenda
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brenda
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and/or vacuole
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and/or cytosol
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CORI3_ARATH
422
0
47039
Swiss-Prot
other Location (Reliability: 4 )
Q84UD0_BRAOL
424
0
47290
TrEMBL
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100000 - 110000
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gel filtration
40000
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4 * 40000, SDS-PAGE
45000
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4 * 45000, SDS-PAGE
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dimer
2 * 43000, SDS-PAGE, two bands of two closely related isoforms. 2 * 47200, calculated
dimer
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2 * 47000, MALDI-TOF, 2 * 48000, SDS-PAGE
tetramer
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4 * 45000, SDS-PAGE
tetramer
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4 * 40000, SDS-PAGE
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3
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complete loss of activity
651551
4 - 8
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30°C, stable for 24 h
651551
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40
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5 min, stable
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10 min, no loss of activity
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5 min, 70% loss of activity
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10 min, 60% loss of activity
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-20°C, little loss of activity during 6 months
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isoform cystine lyase b, rapid purifiaction method
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expression in Escherichia coli
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Ramirez, E.C.; Whitaker, J.R.
Biochemical characterization of cystine lyase from broccoli (Brassica oleracea var. italica)
J. Agric. Food Chem.
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2218-2225
1999
Brassica oleracea var. italica
brenda
Jones, P.R.; Manabe, T.; Awazuhara, M.; Saito, K.
A new member of plant CS-lyases. A cystine lyase from Arabidopsis thaliana
J. Biol. Chem.
278
10291-10296
2003
Brassica oleracea (Q84UD0), Brassica oleracea, Arabidopsis thaliana (Q9SUR6), Arabidopsis thaliana
brenda
Ukai, K.; Sekiya, J.
Rapid purification and characterization of cystine lyase b from broccoli inflorescence
Phytochemistry
51
853-859
1999
Brassica oleracea var. italica
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brenda
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History
Enzyme Nomenclature
4.4.1.35 L-cystine beta-lyase
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