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Literature summary for 1.5.1.8 extracted from

  • Cunha Lima, S.T.; Azevedo, R.A.; Santoro, L.G.; Gaziola, S.A.; Lea, P.J.
    Isolation of the bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase from Phaseolus vulgaris (2003), Amino Acids, 24, 179-186.
    View publication on PubMed
Search for more literature for 1.5.1.8

General Stability

General Stability Organism
lysine 2-oxoglutarate reductase activity is very unstable during purification, following ion-exchange chromatography Phaseolus vulgaris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
190000
-
 bifunctional enzyme lysine 2-oxoglutarate reductase-saccharopine dehydrogenase, gel filtration Phaseolus vulgaris

Organism

Organism UniProt Comment Textmining
Phaseolus vulgaris
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Phaseolus vulgaris

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
 Phaseolus vulgaris
-
hypocotyl
-
 Phaseolus vulgaris
-
leaf
-
 Phaseolus vulgaris
-
pod
-
 Phaseolus vulgaris
-
root
-
 Phaseolus vulgaris
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.98
-
 lysine 2-oxoglutarate reductase activity Phaseolus vulgaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Lys + 2-oxoglutarate + NADPH
-
 Phaseolus vulgaris N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
LOR-SDH
-
 Phaseolus vulgaris
lysine 2-oxoglutarate reductase-saccharopine dehydrogenase bifunctional enzyme Phaseolus vulgaris

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Phaseolus vulgaris