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Literature summary for 1.5.1.8 extracted from

  • Fornazier, R.F.; Gaziola, S.A.; Helm, C.V.; Lea, P.J.; Azevedo, R.A.
    Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds (2005), J. Agric. Food Chem., 53, 1791-1798.
    View publication on PubMed
Search for more literature for 1.5.1.8

General Stability

General Stability Organism
very unstable during the isolation and purification procedure Sorghum bicolor

Organism

Organism UniProt Comment Textmining
Sorghum bicolor
-
 Moench
-
Sorghum bicolor Moench
-
 Moench
-

Purification (Commentary)

Purification (Comment) Organism
partial Sorghum bicolor

Source Tissue

Source Tissue Comment Organism Textmining
endosperm
-
 Sorghum bicolor
-
seed only immature Sorghum bicolor
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
21.34
-
-
 Sorghum bicolor

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
LOR
-
 Sorghum bicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Sorghum bicolor

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.5 pH 6.5: about 60% of maximal activity, pH 9.5: about 60% of maximal activity Sorghum bicolor

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Sorghum bicolor