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Literature summary for 1.4.1.1 extracted from

  • Van Wieren, A.; Cook, R.; Majumdar, S.
    Characterization of alanine dehydrogenase and its effect on Streptomyces coelicolorA3(2) development in liquid culture (2019), J. Mol. Microbiol. Biotechnol., 29, 57-65 .
    View publication on PubMed
Search for more literature for 1.4.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene SCO1773, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli Streptomyces coelicolor

Protein Variants

Protein Variants Comment Organism
additional information construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine + H2O + NAD+ Streptomyces coelicolor
-
 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ Streptomyces coelicolor A3(2)
-
 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ Streptomyces coelicolor ATCC BAA-471
-
 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ Streptomyces coelicolor M145
-
 pyruvate + NH3 + NADH + H+
-
 r
additional information Streptomyces coelicolor the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively ?
-
-
additional information Streptomyces coelicolor A3(2) the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively ?
-
-
additional information Streptomyces coelicolor ATCC BAA-471 the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively ?
-
-
additional information Streptomyces coelicolor M145 the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively ?
-
-

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor Q9S227
-
-
Streptomyces coelicolor A3(2) Q9S227
-
-
Streptomyces coelicolor ATCC BAA-471 Q9S227
-
-
Streptomyces coelicolor M145 Q9S227
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and dialysis Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxobutyrate + NH3 + NADH + H+
-
 Streptomyces coelicolor L-2-aminobutyrate + H2O + NAD+
-
 r
2-oxopentanoate + NH3 + NADH + H+
-
 Streptomyces coelicolor L-norvaline + H2O + NAD+
-
 r
3-hydroxypyruvate + NH3 + NADH + H+
-
 Streptomyces coelicolor L-serine + H2O + NAD+
-
 r
glyoxylate + NH3 + NADH + H+
-
 Streptomyces coelicolor glycine + H2O + NAD+
-
 r
L-2-aminobutyrate + H2O + NAD+
-
 Streptomyces coelicolor 2-oxobutyrate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+
-
 Streptomyces coelicolor pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ reversible oxidative deamination and reductive amination reactions Streptomyces coelicolor pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+
-
 Streptomyces coelicolor A3(2) pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ reversible oxidative deamination and reductive amination reactions Streptomyces coelicolor A3(2) pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+
-
 Streptomyces coelicolor ATCC BAA-471 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ reversible oxidative deamination and reductive amination reactions Streptomyces coelicolor ATCC BAA-471 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+
-
 Streptomyces coelicolor M145 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ reversible oxidative deamination and reductive amination reactions Streptomyces coelicolor M145 pyruvate + NH3 + NADH + H+
-
 r
L-norvaline + H2O + NAD+
-
 Streptomyces coelicolor 2-oxopentanoate + NH3 + NADH + H+
-
 r
L-serine + H2O + NAD+
-
 Streptomyces coelicolor 3-hydroxypyruvate + NH3 + NADH + H+
-
 r
L-valine + H2O + NAD+
-
 Streptomyces coelicolor 3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
 r
L-valine + H2O + NAD+
-
 Streptomyces coelicolor A3(2) 3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
 r
L-valine + H2O + NAD+
-
 Streptomyces coelicolor ATCC BAA-471 3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
 r
L-valine + H2O + NAD+
-
 Streptomyces coelicolor M145 3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
 r
additional information the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively Streptomyces coelicolor ?
-
-
additional information substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine Streptomyces coelicolor ?
-
-
additional information the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively Streptomyces coelicolor A3(2) ?
-
-
additional information substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine Streptomyces coelicolor A3(2) ?
-
-
additional information the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively Streptomyces coelicolor ATCC BAA-471 ?
-
-
additional information substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine Streptomyces coelicolor ATCC BAA-471 ?
-
-
additional information the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively Streptomyces coelicolor M145 ?
-
-
additional information substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine Streptomyces coelicolor M145 ?
-
-
pyruvate + NH3 + NADH + H+
-
 Streptomyces coelicolor L-alanine + H2O + NAD+
-
 r

Synonyms

Synonyms Comment Organism
ALD
-
 Streptomyces coelicolor
L-alanine dehydrogenase
-
 Streptomyces coelicolor
ScALD
-
 Streptomyces coelicolor
SCO1773
-
 Streptomyces coelicolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 35 both reaction directions Streptomyces coelicolor

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 55 decreasing the temperature below 30°C and increasing above 40°C causes sharp decrease in enzyme activities Streptomyces coelicolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 reductive amination Streptomyces coelicolor
9.5
-
 oxidative deamination Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Streptomyces coelicolor
NADH
-
 Streptomyces coelicolor

General Information

General Information Comment Organism
malfunction growth of Streptomyces coelicolor A3(2) is impacted by the deletion of the alanine dehydrogenase (ALD), an essential enzyme that plays a central role in the carbon and nitrogen metabolism. A long lagphase growth followed by a slow exponential growth of Streptomyces coelicolor due to ALD gene deletion is observed in liquid yeast extract mineral salt culture. The slow lag-phase growth is replaced by the normal wild-type like growth by ALD complementation engineering. Deletion mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation Streptomyces coelicolor
metabolism by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source Streptomyces coelicolor

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0017
-
 L-norvaline pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.003
-
 L-valine pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.032
-
 3-hydroxypyruvate pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.041
-
 glyoxylate pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.044
-
 L-serine pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.06
-
 L-2-aminobutyrate pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.11
-
 3-oxovalerate pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
0.61
-
 2-oxobutyrate pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
1.9
-
 pyruvate pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor
2
-
 L-alanine pH 9.0, 30°C, reductive amination reaction Streptomyces coelicolor