Literature summary for 1.2.1.19 extracted from
Yin, Y.; Yang, R.; Wu, J.; Gu, Z.
Partial purification, characterization and cDNA cloning of aminoaldehyde dehydrogenase in germinated soybean (Glycine max L.) (2013), Eur. Food Res. Technol., 237, 731-738 .
No PubMed abstract available
Cloned(Commentary)
Cloned (Comment) |
Organism |
DNA and amino acid sequence determination and analysis, sequence comparisons |
Glycine max |
Inhibitors
Inhibitors |
Comment |
Organism |
Structure |
2-mercaptoethanol |
66% inhibition at 1 mM |
Glycine max |
|
Ba2+ |
30% inhibition at 1 mM |
Glycine max |
|
Cu2+ |
complete inhibition at 1 mM |
Glycine max |
|
EGTA |
7.5% inhibition at 1 mM |
Glycine max |
|
Hg2+ |
62% inhibition at 1 mM |
Glycine max |
|
L-cysteine |
59% inhibition at 1 mM |
Glycine max |
|
Mg2+ |
70% inhibition at 1 mM |
Glycine max |
|
additional information |
EDTA has no significant effect on the enzyme activity |
Glycine max |
|
Ni2+ |
complete inhibition at 1 mM |
Glycine max |
|
Pb2+ |
complete inhibition at 1 mM |
Glycine max |
|
Zn2+ |
92% inhibition at 1 mM |
Glycine max |
|
Metals/Ions
Metals/Ions |
Comment |
Organism |
Structure |
Ca2+ |
no significant effect on the enzyme activity |
Glycine max |
|
Mn2+ |
no significant effect on the enzyme activity |
Glycine max |
|
Organism
Organism |
UniProt |
Comment |
Textmining |
Glycine max |
U5ILS4 |
- |
- |
Purification (Commentary)
Purification (Comment) |
Organism |
native enzyme 27.22fold from germinated seeds by ammonium sulfate fractionation, desalting gel filtration, and anion exchange chromatography |
Glycine max |
Source Tissue
Source Tissue |
Comment |
Organism |
Textmining |
seed |
germinated |
Glycine max |
- |
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
13.71 |
- |
purified native enzyme, substrate 4-aminobutanal, pH 8.0, 37°C |
Glycine max |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
3-aminopropionaldehyde + NAD+ + H2O |
best substrate |
Glycine max |
3-aminopropionate + NADH + 2 H+ |
- |
? |
|
4-aminobutyraldehyde + NAD+ + H2O |
- |
Glycine max |
4-aminobutyrate + NADH + 2 H+ |
- |
? |
|
additional information |
no activity with betaine aldehyde, propionaldehyde, and acetaldehyde |
Glycine max |
? |
- |
? |
|
Subunits
Subunits |
Comment |
Organism |
? |
x * 53720, native enzyme, SDS-PAGE, x * 54790, sequence calculation |
Glycine max |
Synonyms
Synonyms |
Comment |
Organism |
AMADH |
- |
Glycine max |
aminoaldehyde dehydrogenase |
- |
Glycine max |
Temperature Optimum [°C]
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
45 |
- |
- |
Glycine max |
Temperature Range [°C]
Temperature Minimum [°C] |
Temperature Maximum [°C] |
Comment |
Organism |
20 |
60 |
activity range, profile overview |
Glycine max |
Temperature Stability [°C]
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Comment |
Organism |
50 |
60 |
purified enzyme, pH 8.0, rapid inactivation above 50°C, loss of almost 50% activity at 60°C |
Glycine max |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
8 |
- |
- |
Glycine max |
pH Range
pH Minimum |
pH Maximum |
Comment |
Organism |
3 |
9 |
AMADH activity increases with a pH ranging from pH 3.0 to pH 8.0, but it decreases drastically when pH continuously rises from pH 8.0 to pH 10.0. At pH 9.0, the activity decreases by 75% compared to pH 8.0 |
Glycine max |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
NAD+ |
- |
Glycine max |
|
pI Value
Organism |
Comment |
pI Value Maximum |
pI Value |
Glycine max |
sequence calculation |
- |
5.16 |
General Information
General Information |
Comment |
Organism |
evolution |
the enzyme is a member of the aldehyde dehydrogenase 10 family |
Glycine max |