Information on EC 1.5.1.25 - thiomorpholine-carboxylate dehydrogenase

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The expected taxonomic range for this enzyme is: Cetartiodactyla

EC NUMBER
COMMENTARY
1.5.1.25
-
RECOMMENDED NAME
GeneOntology No.
thiomorpholine-carboxylate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
show the reaction diagram
classical ping-pong mechanism
-
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
show the reaction diagram
classical ping-pong mechanism
-
thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thiomorpholine-3-carboxylate:NAD(P)+ 5,6-oxidoreductase
The product is the cyclic imine of the 2-oxoacid corresponding to S-(2-aminoethyl)cysteine. In the reverse direction, a number of other cyclic unsaturated compounds can act as substrates, but more slowly.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ketimine reductase
-
-
-
-
ketimine-reducing enzyme
-
-
-
-
reductase, ketimine
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
115232-54-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cystathionine ketimine + NADH
cyclothionine + NAD+
show the reaction diagram
-
-
-
ir
cystathionine ketimine + NADH
cyclothionine + NAD+
show the reaction diagram
-
-
-
-
?
cystathionine ketimine + NADPH
cyclothionine + NADP+
show the reaction diagram
-
-
-
ir
cystathionine ketimine + NADPH
cyclothionine + NADP+
show the reaction diagram
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADH
? + NAD+
show the reaction diagram
-
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADH
? + NAD+
show the reaction diagram
-
-
-
-
?
DELTA1-piperideine 2-carboxylate + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
ir
DELTA1-piperideine 2-carboxylate + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
show the reaction diagram
-
-
-
ir
lanthionine ketimine + NADH
1,4-thiomorpholine 3,5-dicarboxylic acid + NAD+
show the reaction diagram
-
-
-
-
?
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
show the reaction diagram
-
-
-
ir
lanthionine ketimine + NADPH
1,4-thiomorpholine 3,5-dicarboxylic acid + NADP+
show the reaction diagram
-
-
-
-
?
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
show the reaction diagram
-
-
-
-
?
S-aminoethylcysteine ketimine + NADH
1,4-thiomorpholine 3-carboxylic acid + NAD+
show the reaction diagram
-
-
L-enantiomer
ir
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
show the reaction diagram
-
-
-
ir
S-aminoethylcysteine ketimine + NADPH
1,4-thiomorpholine 3-carboxylic acid + NADP+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
NADH
-
reduction rate for cystathionine ketimine, lanthionine ketimine and DELTA1-piperidine 2-carboxylate is higher with NADPH than with NADH. Reduction rate for S-aminoethylcysteine with NADH is higher than with NADPH
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
NADPH
-
reduction rate for cystathionine ketimine, lanthionine ketimine and DELTA1-piperidine 2-carboxylate is higher with NADPH than with NADH. Reduction rate for S-aminoethylcysteine with NADH is higher than with NADPH
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Triton X-100
-
irreversible inactivation
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3
-
Cystathionine ketimine
-
reaction with NADH
10
-
Cystathionine ketimine
-
reaction with NADPH
0.33
-
DELTA1-Piperidine 2-carboxylate
-
reaction with DELTA1-piperidine-2-carboxylate
0.47
-
Lanthionine ketimine
-
reaction with NADH
1.17
-
Lanthionine ketimine
-
reaction with NADPH
0.015
-
NADH
-
reaction with DELTA1-piperidine 2-carboxylate
0.027
-
NADH
-
reaction with S-aminoethylcysteine ketimine
0.26
-
NADH
-
reaction with DELTA1-piperidine 2-carboxylate
0.077
-
S-Aminoethylcysteine ketimine
-
-
0.24
-
S-Aminoethylcysteine ketimine
-
reaction with NADH
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16.3
-
-
-
16.6
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
reaction with S-aminoethylcysteine ketimine or lanthionine ketimine, acetate buffer or phosphate buffer
4.5
-
-
reaction with lanthionine ketimine and NADPH
5
-
-
-
5
-
-
reaction with S-aminoethylcysteine ketimine and NADH, cystathionine ketimine and NADPH or 1-piperidine 2-carboxylate and NADPH
6
-
-
reaction with cystathionine ketimine, acetate buffer or phosphate buffer
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
localized prevalently in cerebellum and cerebral cortices
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
73000
-
-
gel filtration
76000
-
-
non-denaturing PAGE
100000
-
-
non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 45000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4°C, purified enzyme is stable for at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE