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Literature summary for 1.1.1.191 extracted from

  • Ludwig-Muller, J.; Hilgenberg, W.
    Purification of NADPH-specific indole-3-acetaldehyde reductase from Cucumis sativus by two-dimensional native polyacrylamide gel electrophoresis (1989), Physiol. Plant., 77, 613-619.
No PubMed abstract available
Search for more literature for 1.1.1.191

Inhibitors

Inhibitors Comment Organism Structure
dihydroxyacetonephosphate non-competitive inhibition, Ki: 0.35 mM Cucumis sativus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.025
-
 Indole-3-acetaldehyde
-
 Cucumis sativus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
indole-3-acetaldehyde + NADPH Cucumis sativus substrates hold key positions in the regulation of indole-3-acetic acid content in higher plants indole-3-ethanol + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Cucumis sativus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, chromatography steps, native PAGE Cucumis sativus

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
 Cucumis sativus
-
seed
-
 Cucumis sativus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.002
-
 partial purified from seedlings Cucumis sativus
0.014
-
 partial purified from fruits Cucumis sativus
0.04
-
 cytosolic fraction Cucumis sativus
0.24
-
 purified from fruits Cucumis sativus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole-3-acetaldehyde + NADPH substrates hold key positions in the regulation of indole-3-acetic acid content in higher plants Cucumis sativus indole-3-ethanol + NADP+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Cucumis sativus