BRENDA - Enzyme Database
show all sequences of 1.5.1.25

Purification and characterization of a ketimine-reducing enzyme

Nardini, M.; Ricci, G.; Caccuri, A.M.; Solinas, S.P.; Vesci, L.; Cavallini, D.; Eur. J. Biochem. 173, 689-694 (1988)

Data extracted from this reference:

General Stability
General Stability
Organism
irreversible inactivation at protein concentration below 1 mg/ml. Complete loss of activity after 24 h at 4C. Higher protein concentrations or 10% glycerol prevent enzyme inactivation. 30% loss of activity aftter 7 days at 4C
Sus scrofa
Inhibitors
Inhibitors
Commentary
Organism
Structure
Triton X-100
irreversible inactivation
Sus scrofa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.027
-
NADH
reaction with S-aminoethylcysteine ketimine
Sus scrofa
0.077
-
S-Aminoethylcysteine ketimine
-
Sus scrofa
0.47
-
Lanthionine ketimine
reaction with NADH
Sus scrofa
3
-
Cystathionine ketimine
reaction with NADH
Sus scrofa
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
73000
-
gel filtration
Sus scrofa
76000
-
non-denaturing PAGE
Sus scrofa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sus scrofa
-
-
-
Purification (Commentary)
Commentary
Organism
-
Sus scrofa
Reaction
Reaction
Commentary
Organism
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
classical ping-pong mechanism
Sus scrofa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Sus scrofa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
16.3
-
-
Sus scrofa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cystathionine ketimine + NADH
-
440358
Sus scrofa
cyclothionine + NAD+
-
440358
Sus scrofa
ir
cystathionine ketimine + NADPH
-
440358
Sus scrofa
cyclothionine + NADP+
-
440358
Sus scrofa
ir
DELTA1-piperideine 2-carboxylate + NADH
-
440358
Sus scrofa
? + NAD+
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADPH
-
440358
Sus scrofa
? + NADP+
-
-
-
ir
lanthionine ketimine + NADH
-
440358
Sus scrofa
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
-
440358
Sus scrofa
ir
lanthionine ketimine + NADPH
-
440358
Sus scrofa
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
-
440358
Sus scrofa
ir
S-aminoethylcysteine ketimine + NADH
-
440358
Sus scrofa
1,4-thiomorpholine 3-carboxylic acid + NAD+
L-enantiomer
440358
Sus scrofa
ir
S-aminoethylcysteine ketimine + NADPH
-
440358
Sus scrofa
1,4-thiomorpholine 3-carboxylic acid + NADP+
-
440358
Sus scrofa
ir
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.5
-
reaction with S-aminoethylcysteine ketimine or lanthionine ketimine, acetate buffer or phosphate buffer
Sus scrofa
5
-
-
Sus scrofa
6
-
reaction with cystathionine ketimine, acetate buffer or phosphate buffer
Sus scrofa
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
NADH and NADPH show equal activity with cystathionine ketimine as substrate. Reduction of lanthionine ketimine with NADPH is faster than reduction with NADH. Reduction of S-aminoethylcysteine with NADH is faster than reduction with NADPH
Sus scrofa
NADPH
NADH and NADPH show equal activity with cystathionine ketimine as substrate. Reduction of lanthionine ketimine with NADPH is faster than reduction with NADH. Reduction of S-aminoethylcysteine with NADH is faster than reduction with NADPH
Sus scrofa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
NADH and NADPH show equal activity with cystathionine ketimine as substrate. Reduction of lanthionine ketimine with NADPH is faster than reduction with NADH. Reduction of S-aminoethylcysteine with NADH is faster than reduction with NADPH
Sus scrofa
NADPH
NADH and NADPH show equal activity with cystathionine ketimine as substrate. Reduction of lanthionine ketimine with NADPH is faster than reduction with NADH. Reduction of S-aminoethylcysteine with NADH is faster than reduction with NADPH
Sus scrofa
General Stability (protein specific)
General Stability
Organism
irreversible inactivation at protein concentration below 1 mg/ml. Complete loss of activity after 24 h at 4C. Higher protein concentrations or 10% glycerol prevent enzyme inactivation. 30% loss of activity aftter 7 days at 4C
Sus scrofa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Triton X-100
irreversible inactivation
Sus scrofa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.027
-
NADH
reaction with S-aminoethylcysteine ketimine
Sus scrofa
0.077
-
S-Aminoethylcysteine ketimine
-
Sus scrofa
0.47
-
Lanthionine ketimine
reaction with NADH
Sus scrofa
3
-
Cystathionine ketimine
reaction with NADH
Sus scrofa
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
73000
-
gel filtration
Sus scrofa
76000
-
non-denaturing PAGE
Sus scrofa
Purification (Commentary) (protein specific)
Commentary
Organism
-
Sus scrofa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Sus scrofa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
16.3
-
-
Sus scrofa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
cystathionine ketimine + NADH
-
440358
Sus scrofa
cyclothionine + NAD+
-
440358
Sus scrofa
ir
cystathionine ketimine + NADPH
-
440358
Sus scrofa
cyclothionine + NADP+
-
440358
Sus scrofa
ir
DELTA1-piperideine 2-carboxylate + NADH
-
440358
Sus scrofa
? + NAD+
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADPH
-
440358
Sus scrofa
? + NADP+
-
-
-
ir
lanthionine ketimine + NADH
-
440358
Sus scrofa
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
-
440358
Sus scrofa
ir
lanthionine ketimine + NADPH
-
440358
Sus scrofa
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
-
440358
Sus scrofa
ir
S-aminoethylcysteine ketimine + NADH
-
440358
Sus scrofa
1,4-thiomorpholine 3-carboxylic acid + NAD+
L-enantiomer
440358
Sus scrofa
ir
S-aminoethylcysteine ketimine + NADPH
-
440358
Sus scrofa
1,4-thiomorpholine 3-carboxylic acid + NADP+
-
440358
Sus scrofa
ir
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.5
-
reaction with S-aminoethylcysteine ketimine or lanthionine ketimine, acetate buffer or phosphate buffer
Sus scrofa
5
-
-
Sus scrofa
6
-
reaction with cystathionine ketimine, acetate buffer or phosphate buffer
Sus scrofa
Other publictions for EC 1.5.1.25
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741584
Hallen
Ketimine reductase/CRYM catal ...
Homo sapiens
Amino Acids
47
2457-2461
2015
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
7
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
743354
Hallen
Insights into enzyme catalysi ...
Bos taurus, Homo sapiens, Mus musculus
Neurochem. Res.
40
1252-1266
2015
-
-
-
-
-
-
20
5
3
-
-
15
-
3
-
-
-
3
-
3
-
-
16
-
1
-
-
4
3
-
-
3
6
-
1
-
-
-
3
-
-
-
1
20
6
5
3
-
-
15
-
-
-
-
-
3
-
-
16
-
1
-
-
4
3
-
-
-
-
4
4
-
4
4
741580
Hallen
Lysine metabolism in mammalia ...
Bos taurus, Homo sapiens, Macropus giganteus, Mus musculus, Rattus norvegicus, Sus scrofa
Amino Acids
45
1249-1272
2013
-
-
-
-
-
-
6
-
6
-
-
9
-
6
-
-
4
-
-
16
1
-
9
-
-
-
-
-
1
-
-
6
1
-
-
-
-
-
6
-
-
-
-
6
1
-
6
-
-
9
-
-
-
4
-
16
1
-
9
-
-
-
-
-
1
-
-
-
2
14
14
2
-
-
440358
Nardini
Purification and characterizat ...
Sus scrofa
Eur. J. Biochem.
173
689-694
1988
-
-
-
-
-
1
1
4
-
-
2
-
-
3
-
-
1
1
-
1
1
-
8
-
-
-
-
-
3
-
-
2
-
-
-
-
-
-
2
-
-
1
-
1
-
4
-
-
2
-
-
-
-
1
-
1
1
-
8
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
440359
Nardini
Bovine brain ketimine reductas ...
Bos taurus
Biochim. Biophys. Acta
957
286-292
1988
-
-
-
-
-
-
-
6
1
-
2
-
-
1
-
-
1
1
-
1
1
1
8
1
-
-
-
-
2
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
6
1
-
2
-
-
-
-
1
-
1
1
1
8
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-