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Literature summary for 1.4.1.19 extracted from

  • Vackova, K.; Mehta, A.; Kutacek, M.
    Tryptophan aminotransferase and tryptophan dehydrogenase activities in some cell compartments of spinach leaves: the effect of calcium ions on tryptophan dehydrogenase (1985), Biol. Plant., 27, 154-158.
No PubMed abstract available

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Spinacia oleracea 9507
-
cytoplasm
-
Spinacia oleracea 5737
-
additional information enzyme occurs in cytoplasm, chloroplast and pellet of remaining organelles sedimenting at 97000 * g Spinacia oleracea
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ optimal activation at 0.8 mM Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
spinach
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.014
-
activity in organelles, cofactor NAD+, deamination of L-tryptophan Spinacia oleracea
0.0155
-
activity in organelles, cofactor NADP+, deamination of L-tryptophan Spinacia oleracea
0.0359
-
activity in organelles, cofactor NADH, amination of L-tryptophan Spinacia oleracea
0.648
-
activity in organelles, cofactor NADPH, amination of L-tryptophan Spinacia oleracea

Cofactor

Cofactor Comment Organism Structure
NAD(P)+
-
Spinacia oleracea
NAD(P)H effect of NADPH compared to NADH is distinctly higher Spinacia oleracea