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Literature summary for 3.1.1.49 extracted from

  • Nurmann, G.; Strack, D.
    Sinapine esterase. 1. Characterization of sinapine esterase from cotyledons of Raphanus sativus (1979), Z. Naturforsch. C, 34, 715-720.
No PubMed abstract available
Search for more literature for 3.1.1.49

Activating Compound

Activating Compound Comment Organism Structure
Acetylcholine stimulation Raphanus sativus

Inhibitors

Inhibitors Comment Organism Structure
choline chloride 100 mM 60% inhibition Raphanus sativus
diethyl p-nitrophenylphosphate
-
 Raphanus sativus
diisopropyl fluorophosphate
-
 Raphanus sativus
physostigmine i.e. eserine Raphanus sativus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0195
-
 Sinapoylcholine
-
 Raphanus sativus

Organism

Organism UniProt Comment Textmining
Raphanus sativus
-
 red radish
-

Purification (Commentary)

Purification (Comment) Organism
-
 Raphanus sativus

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
 Raphanus sativus
-
seedling
-
 Raphanus sativus
-

Storage Stability

Storage Stability Organism
-20°C, tricine buffer, several weeks Raphanus sativus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sinapoylcholine + H2O
-
 Raphanus sativus sinapic acid + choline
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
 Raphanus sativus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
24 40 less than 50% of maximal activity above and below Raphanus sativus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Raphanus sativus

pH Range

pH Minimum pH Maximum Comment Organism
5.5 10 less than 50% of maximal activity above and below Raphanus sativus