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Literature summary extracted from

  • Nardini, M.; Ricci, G.; Caccuri, A.M.; Solinas, S.P.; Vesci, L.; Cavallini, D.
    Purification and characterization of a ketimine-reducing enzyme (1988), Eur. J. Biochem., 173, 689-694.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.5.1.25 irreversible inactivation at protein concentration below 1 mg/ml. Complete loss of activity after 24 h at 4°C. Higher protein concentrations or 10% glycerol prevent enzyme inactivation. 30% loss of activity aftter 7 days at 4°C Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.5.1.25 Triton X-100 irreversible inactivation Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.1.25 0.027
-
 NADH reaction with S-aminoethylcysteine ketimine Sus scrofa
1.5.1.25 0.077
-
 S-Aminoethylcysteine ketimine
-
 Sus scrofa
1.5.1.25 0.47
-
 Lanthionine ketimine reaction with NADH Sus scrofa
1.5.1.25 3
-
 Cystathionine ketimine reaction with NADH Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.25 73000
-
 gel filtration Sus scrofa
1.5.1.25 76000
-
 non-denaturing PAGE Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.25 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.25
-
 Sus scrofa

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.1.25 thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+ classical ping-pong mechanism Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.25 kidney
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.25 16.3
-
-
 Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.25 cystathionine ketimine + NADH
-
 Sus scrofa cyclothionine + NAD+
-
 ir
1.5.1.25 cystathionine ketimine + NADPH
-
 Sus scrofa cyclothionine + NADP+
-
 ir
1.5.1.25 DELTA1-piperideine 2-carboxylate + NADH
-
 Sus scrofa ? + NAD+
-
 ir
1.5.1.25 DELTA1-piperideine 2-carboxylate + NADPH
-
 Sus scrofa ? + NADP+
-
 ir
1.5.1.25 lanthionine ketimine + NADH
-
 Sus scrofa 1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
-
 ir
1.5.1.25 lanthionine ketimine + NADPH
-
 Sus scrofa 1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
-
 ir
1.5.1.25 S-aminoethylcysteine ketimine + NADH
-
 Sus scrofa 1,4-thiomorpholine 3-carboxylic acid + NAD+ L-enantiomer ir
1.5.1.25 S-aminoethylcysteine ketimine + NADPH
-
 Sus scrofa 1,4-thiomorpholine 3-carboxylic acid + NADP+
-
 ir

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.25 4.5
-
 reaction with S-aminoethylcysteine ketimine or lanthionine ketimine, acetate buffer or phosphate buffer Sus scrofa
1.5.1.25 5
-
-
 Sus scrofa
1.5.1.25 6
-
 reaction with cystathionine ketimine, acetate buffer or phosphate buffer Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.25 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
1.5.1.25 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