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Literature summary extracted from

  • Ishige, T.; Tani, A.; Sakai, Y.; Kato, N.
    Long-chain aldehyde dehydrogenase that participates in n-alkane utilization and wax ester synthesis in Acinetobacter sp. strain M-1 (2000), Appl. Environ. Microbiol., 66, 3481-3486.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.48 gene ald1 cloned from the chromosomal DNA of the bacterium and expressed in Escherichia coli Acinetobacter sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.48 Ag+ 1 mM causes complete inhibition Acinetobacter sp.
1.2.1.48 Cu2+ 1 mM causes 63% inhibition Acinetobacter sp.
1.2.1.48 Fe3+ 1 mM causes complete inhibition Acinetobacter sp.
1.2.1.48 Hg2+ 1 mM causes complete inhibition Acinetobacter sp.
1.2.1.48 iodoacetate 1 mM causes strong inhibition Acinetobacter sp.
1.2.1.48 Mn2+ 1 mM causes 37% inhibition Acinetobacter sp.
1.2.1.48 N-ethylmaleimide 1 mM causes complete inhibition Acinetobacter sp.
1.2.1.48 p-chloromercuribenzoate 1 mM causes complete inhibition Acinetobacter sp.
1.2.1.48 Pb2+ 1 mM causes complete inhibition Acinetobacter sp.
1.2.1.48 Zn2+ 1 mM causes 44% inhibition Acinetobacter sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.48 Mg2+ 1 mM causes 35% increase in activity Acinetobacter sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.48 55000
-
 4 * 55000, SDS-PAGE, recombinant enzyme from Escherichia coli Acinetobacter sp.
1.2.1.48 55496
-
 x * 55496, calculated from the deduced amino acid sequence Acinetobacter sp.
1.2.1.48 232000
-
 gel filtration, purified recombinant enzyme from Escherichia coli Acinetobacter sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.48 long-chain aldehyde + NAD+ Acinetobacter sp. the enzyme plays a significant role in n-alkane utilization, especially in intracellular wax ester synthesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.48 Acinetobacter sp.
-
-
-
1.2.1.48 Acinetobacter sp. M-1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.48 including chromatography in a Resource Q column, recombinant enzyme from Escherichia coli also purified Acinetobacter sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.48 10.9
-
 purified recombinant enzyme from Escherichia coli, tetradecanal used as substrate Acinetobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.48 benzaldehyde + NAD+ + H2O 66% activity toward tetradecanal Acinetobacter sp. benzoate + NADH + H+
-
 ?
1.2.1.48 benzaldehyde + NAD+ + H2O 66% activity toward tetradecanal Acinetobacter sp. M-1 benzoate + NADH + H+
-
 ?
1.2.1.48 cis-9-hexadecenal + NAD+ + H2O 31% activity toward tetradecanal Acinetobacter sp. cis-9-hexadecenoic acid + NADH
-
 ?
1.2.1.48 long-chain aldehyde + NAD+ the enzyme plays a significant role in n-alkane utilization, especially in intracellular wax ester synthesis Acinetobacter sp. ?
-
 ?
1.2.1.48 long-chain aldehyde + NAD+ + H2O
-
 Acinetobacter sp. long-chain acid anion + NADH
-
 ?
1.2.1.48 long-chain aldehyde + NAD+ + H2O
-
 Acinetobacter sp. M-1 long-chain acid anion + NADH
-
 ?
1.2.1.48 m-fluorobenzaldehyde + NAD+ + H2O
-
 Acinetobacter sp. m-fluorobenzoic acid + NADH + H+
-
 ?
1.2.1.48 m-methylbenzaldehyde + NAD+ + H2O 36% activity toward tetradecanal Acinetobacter sp. m-methylbenzoic acid + NADH
-
 ?
1.2.1.48 additional information not: acetaldehyde Acinetobacter sp. ?
-
 ?
1.2.1.48 additional information not: propionaldehyde Acinetobacter sp. ?
-
 ?
1.2.1.48 additional information not: acetaldehyde Acinetobacter sp. M-1 ?
-
 ?
1.2.1.48 additional information not: propionaldehyde Acinetobacter sp. M-1 ?
-
 ?
1.2.1.48 o-fluorobenzaldehyde + NAD+ + H2O
-
 Acinetobacter sp. o-fluorobenzoic acid + NADH + H+
-
 ?
1.2.1.48 p-chlorobenzaldehyde + NAD+ + H2O
-
 Acinetobacter sp. p-chlorobenzoic acid + NADH + H+
-
 ?
1.2.1.48 p-fluorobenzaldehyde + NAD+ + H2O
-
 Acinetobacter sp. p-fluorobenzoic acid + NADH + H+
-
 ?
1.2.1.48 tetradecanal + NAD+ + H2O highest activity Acinetobacter sp. tetradecanoic acid + NADH
-
 ?
1.2.1.48 tetradecanal + NAD+ + H2O highest activity Acinetobacter sp. M-1 tetradecanoic acid + NADH
-
 ?
1.2.1.48 trans-2-decenal + NAD+ + H2O 32% activity toward tetradecanal Acinetobacter sp. trans-2-decenoic acid + NADH
-
 ?
1.2.1.48 trans-cinnamaldehyde + NAD+ + H2O 38% activity toward tetradecanal Acinetobacter sp. trans-cinnamic acid + NADH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.48 ? x * 55496, calculated from the deduced amino acid sequence Acinetobacter sp.
1.2.1.48 tetramer 4 * 55000, SDS-PAGE, recombinant enzyme from Escherichia coli Acinetobacter sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.48 43
-
-
 Acinetobacter sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.48 30
-
 30 min, pH 7.5 to 9.0, more than 90% of activity remains Acinetobacter sp.
1.2.1.48 60
-
 30 min, 90% of activity remains Acinetobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.48 9.5
-
-
 Acinetobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.48 NAD+ the enzyme does not use NADP+ as cofactor Acinetobacter sp.