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Literature summary for 1.2.1.22 extracted from

  • Wu, X.; Xu, L.; Yan, M.
    A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli (2016), Biosci. Biotechnol. Biochem., 80, 2306-2310 .
    View publication on PubMed
Search for more literature for 1.2.1.22

Cloned(Commentary)

Cloned (Comment) Organism
gene aldA, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
H449R site-directed mutagenesis Escherichia coli
L158Y site-directed mutagenesis Escherichia coli
additional information calculated Gibbs free energy of protein-substrate interaction of enzyme mutants with D-glyceraldehyde as substrate Escherichia coli
N286A site-directed mutagenesis Escherichia coli
N286C site-directed mutagenesis Escherichia coli
N286D site-directed mutagenesis Escherichia coli
N286E site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal Escherichia coli
N286F site-directed mutagenesis Escherichia coli
N286G site-directed mutagenesis Escherichia coli
N286H site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde Escherichia coli
N286I site-directed mutagenesis Escherichia coli
N286K site-directed mutagenesis Escherichia coli
N286L site-directed mutagenesis Escherichia coli
N286M site-directed mutagenesis Escherichia coli
N286P site-directed mutagenesis Escherichia coli
N286Q site-directed mutagenesis Escherichia coli
N286R site-directed mutagenesis Escherichia coli
N286S site-directed mutagenesis Escherichia coli
N286T site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme and is able to oxidate glyceraldehyde and methylglyoxal, as well as acetaldehyde Escherichia coli
N286V site-directed mutagenesis Escherichia coli
N286W site-directed mutagenesis Escherichia coli
N286Y site-directed mutagenesis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-lactaldehyde + NAD+ + H2O Escherichia coli
-
 (S)-lactate + NADH + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P25553
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by anion exchange chromatography to near homogeneity Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.74
-
 purified recombinant enzyme, pH 7.0, 37°C, substrate (S)-lactaldehyde Escherichia coli
1.18
-
 purified recombinant mutant N286H, pH 7.0, 37°C, substrate (S)-lactaldehyde Escherichia coli
1.78
-
 purified recombinant mutant N286E, pH 7.0, 37°C, substrate (S)-lactaldehyde Escherichia coli
2.18
-
 purified recombinant mutant N286T, pH 7.0, 37°C, substrate (S)-lactaldehyde Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-lactaldehyde + NAD+ + H2O
-
 Escherichia coli (S)-lactate + NADH + 2 H+
-
 ?
additional information residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification. The wild-type enzyme is not active with D-glyceraldehyde, methylglyoxal, acetaldehyde, L-lactate, or benzaldehyde Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
? x * 52200, recombinant enzyme, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
AldA
-
 Escherichia coli
L-lactaldehyde dehydrogenase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15
-
 recombinant mutant N286H Escherichia coli
40
-
 recombinant wild-type enzyme Escherichia coli
45
-
 recombinant mutants N286T and N286E Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40 55 purified recombinant wild-type enzyme is stable at 40°C after incubation for 1 h, but its stability decreases rapidly above 40°C. The mutants N286E and N286H show the same stability, decreasing rapidly above 40°C and exhibiting 20% and 40% of their maximum activity at 45°C, respectively. In contrast, mutant N286T is stable above 50°C and retains 60% of its maximum activity at 55°C after incubation for 1 h Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli

General Information

General Information Comment Organism
additional information residue Asn286 of L-lactaldehyde dehydrogenase plays an important structure role to substrate identification, molecular structure modeling of wild-type enzyme and N286 mutants Escherichia coli