Cloned (Comment) | Organism |
---|---|
gene ald1 cloned from the chromosomal DNA of the bacterium and expressed in Escherichia coli | Acinetobacter sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ag+ | 1 mM causes complete inhibition | Acinetobacter sp. | |
Cu2+ | 1 mM causes 63% inhibition | Acinetobacter sp. | |
Fe3+ | 1 mM causes complete inhibition | Acinetobacter sp. | |
Hg2+ | 1 mM causes complete inhibition | Acinetobacter sp. | |
iodoacetate | 1 mM causes strong inhibition | Acinetobacter sp. | |
Mn2+ | 1 mM causes 37% inhibition | Acinetobacter sp. | |
N-ethylmaleimide | 1 mM causes complete inhibition | Acinetobacter sp. | |
p-chloromercuribenzoate | 1 mM causes complete inhibition | Acinetobacter sp. | |
Pb2+ | 1 mM causes complete inhibition | Acinetobacter sp. | |
Zn2+ | 1 mM causes 44% inhibition | Acinetobacter sp. |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | 1 mM causes 35% increase in activity | Acinetobacter sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
4 * 55000, SDS-PAGE, recombinant enzyme from Escherichia coli | Acinetobacter sp. |
55496 | - |
x * 55496, calculated from the deduced amino acid sequence | Acinetobacter sp. |
232000 | - |
gel filtration, purified recombinant enzyme from Escherichia coli | Acinetobacter sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
long-chain aldehyde + NAD+ | Acinetobacter sp. | the enzyme plays a significant role in n-alkane utilization, especially in intracellular wax ester synthesis | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter sp. | - |
- |
- |
Acinetobacter sp. M-1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
including chromatography in a Resource Q column, recombinant enzyme from Escherichia coli also purified | Acinetobacter sp. |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
10.9 | - |
purified recombinant enzyme from Escherichia coli, tetradecanal used as substrate | Acinetobacter sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
benzaldehyde + NAD+ + H2O | 66% activity toward tetradecanal | Acinetobacter sp. | benzoate + NADH + H+ | - |
? | |
benzaldehyde + NAD+ + H2O | 66% activity toward tetradecanal | Acinetobacter sp. M-1 | benzoate + NADH + H+ | - |
? | |
cis-9-hexadecenal + NAD+ + H2O | 31% activity toward tetradecanal | Acinetobacter sp. | cis-9-hexadecenoic acid + NADH | - |
? | |
long-chain aldehyde + NAD+ | the enzyme plays a significant role in n-alkane utilization, especially in intracellular wax ester synthesis | Acinetobacter sp. | ? | - |
? | |
long-chain aldehyde + NAD+ + H2O | - |
Acinetobacter sp. | long-chain acid anion + NADH | - |
? | |
long-chain aldehyde + NAD+ + H2O | - |
Acinetobacter sp. M-1 | long-chain acid anion + NADH | - |
? | |
m-fluorobenzaldehyde + NAD+ + H2O | - |
Acinetobacter sp. | m-fluorobenzoic acid + NADH + H+ | - |
? | |
m-methylbenzaldehyde + NAD+ + H2O | 36% activity toward tetradecanal | Acinetobacter sp. | m-methylbenzoic acid + NADH | - |
? | |
additional information | not: acetaldehyde | Acinetobacter sp. | ? | - |
? | |
additional information | not: propionaldehyde | Acinetobacter sp. | ? | - |
? | |
additional information | not: acetaldehyde | Acinetobacter sp. M-1 | ? | - |
? | |
additional information | not: propionaldehyde | Acinetobacter sp. M-1 | ? | - |
? | |
o-fluorobenzaldehyde + NAD+ + H2O | - |
Acinetobacter sp. | o-fluorobenzoic acid + NADH + H+ | - |
? | |
p-chlorobenzaldehyde + NAD+ + H2O | - |
Acinetobacter sp. | p-chlorobenzoic acid + NADH + H+ | - |
? | |
p-fluorobenzaldehyde + NAD+ + H2O | - |
Acinetobacter sp. | p-fluorobenzoic acid + NADH + H+ | - |
? | |
tetradecanal + NAD+ + H2O | highest activity | Acinetobacter sp. | tetradecanoic acid + NADH | - |
? | |
tetradecanal + NAD+ + H2O | highest activity | Acinetobacter sp. M-1 | tetradecanoic acid + NADH | - |
? | |
trans-2-decenal + NAD+ + H2O | 32% activity toward tetradecanal | Acinetobacter sp. | trans-2-decenoic acid + NADH | - |
? | |
trans-cinnamaldehyde + NAD+ + H2O | 38% activity toward tetradecanal | Acinetobacter sp. | trans-cinnamic acid + NADH | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 55496, calculated from the deduced amino acid sequence | Acinetobacter sp. |
tetramer | 4 * 55000, SDS-PAGE, recombinant enzyme from Escherichia coli | Acinetobacter sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
43 | - |
- |
Acinetobacter sp. |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
30 min, pH 7.5 to 9.0, more than 90% of activity remains | Acinetobacter sp. |
60 | - |
30 min, 90% of activity remains | Acinetobacter sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.5 | - |
- |
Acinetobacter sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | the enzyme does not use NADP+ as cofactor | Acinetobacter sp. |