Information on EC 4.4.1.35 - cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.4.1.35
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RECOMMENDED NAME
GeneOntology No.
cis-3-hydroxy-L-proline hydro-lyase (1-pyrroline-2-carboxylate-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-aminoprop-2-enoate = 2-iminopropanoate
show the reaction diagram
(1b), spontaneous
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2-iminopropanoate + H2O = pyruvate + NH3
show the reaction diagram
(1c), spontaneous
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L-cystine + H2O = L-thiocysteine + pyruvate + NH3
show the reaction diagram
overall reaction
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L-cystine = L-thiocysteine + 2-aminoprop-2-enoate
show the reaction diagram
(1a)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
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SYSTEMATIC NAME
IUBMB Comments
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminoprop-2-enoate
2-iminopropanoate
show the reaction diagram
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spontaneous partial reaction
-
?
2-iminopropanoate + H2O
pyruvate + NH3
show the reaction diagram
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spontaneous partial reaction
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?
L-cysteine S-sulfate + H2O
?
show the reaction diagram
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-
-
-
?
L-cystine
L-thiocysteine + 2-aminoprop-2-enoate
show the reaction diagram
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-
-
-
?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
show the reaction diagram
L-djenkolic acid + H2O
?
show the reaction diagram
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18-24% of the activity with L-cystine
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?
S-ethyl L-cysteine + H2O
?
show the reaction diagram
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71% of the activity with L-cystine
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?
S-ethyl L-cysteine sulfoxide + H2O
?
show the reaction diagram
S-methyl L-cysteine + H2O
?
show the reaction diagram
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29% of the activity with L-cystine
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?
S-methyl L-cysteine sulfoxide + H2O
?
show the reaction diagram
S-propyl L-cysteine + H2O
?
show the reaction diagram
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29% of the activity with L-cystine
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-aminoprop-2-enoate
2-iminopropanoate
show the reaction diagram
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spontaneous partial reaction
-
?
2-iminopropanoate + H2O
pyruvate + NH3
show the reaction diagram
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spontaneous partial reaction
-
?
L-cystine
L-thiocysteine + 2-aminoprop-2-enoate
show the reaction diagram
-
-
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?
L-cystine + H2O
L-thiocysteine + pyruvate + NH3
show the reaction diagram
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overall reaction
-
?
S-ethyl L-cysteine sulfoxide + H2O
?
show the reaction diagram
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48% of the activity with L-cystine
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?
S-methyl L-cysteine sulfoxide + H2O
?
show the reaction diagram
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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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
hydroxylamine
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0812 - 2.32
L-cystine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
L-cysteine
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pH 8.4, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 11
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more than 50% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000 - 110000
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gel filtration
160000
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gel filtration
186000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 40000, SDS-PAGE; 4 * 45000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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complete loss of activity
651551
4 - 8
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30C, stable for 24 h
651551
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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10 min, no loss of activity; 5 min, stable
50
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10 min, 60% loss of activity; 5 min, 70% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, little loss of activity during 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; isoform cystine lyase b, rapid purifiaction method
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli