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Literature summary extracted from

  • Hu, X.; Bai, Y.; Fan, T.P.; Zheng, X.; Cai, Y.
    A novel type alanine dehydrogenase from Helicobacter aurati molecular characterization and application (2020), Int. J. Biol. Macromol., 161, 636-642 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.1 gene ald, phylogenetic tree, recombinant expression of His-tagged isozyme HAADH1 in Escherichia coli strain BL21(DE3) Helicobacter aurati
1.4.1.1 gene CQA66_00465, phylogenetic tree, recombinant expression of His-tagged isozyme HAADH2 in Escherichia coli strain BL21(DE3) Helicobacter aurati

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.1 0.56
-
pyruvate recombinant enzyme, pH 9.0, 55°C Helicobacter aurati
1.4.1.1 2.23
-
L-alanine recombinant enzyme, pH 8.0, 55°C Helicobacter aurati

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.1.1 L-alanine + H2O + NAD+ Helicobacter aurati
-
pyruvate + NH3 + NADH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.1 Helicobacter aurati A0A3D8J648
-
-
1.4.1.1 Helicobacter aurati A0A3D8J924
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.1 recombinant His-tagged isozyme HAADH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Helicobacter aurati
1.4.1.1 recombinant His-tagged isozyme HAADH2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Helicobacter aurati

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.1 26
-
purified recombinant enzyme, pH 9.0, 55°C Helicobacter aurati
1.4.1.1 268
-
purified recombinant enzyme, pH 9.0, 55°C Helicobacter aurati

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.1 2-oxobutyrate + NH3 + NADH + H+
-
Helicobacter aurati L-2-aminobutyrate + H2O + NAD+
-
r
1.4.1.1 2-oxoglutarate + NH3 + NADH + H+
-
Helicobacter aurati L-glutamate + H2O + NAD+
-
r
1.4.1.1 3-fluoropyruvate + NH3 + NADH + H+ recombinant enzyme in whole-cell catalysis at 25°C Helicobacter aurati 3-fluoro-L-alanine + H2O + NAD+
-
r
1.4.1.1 glyoxylate + NH3 + NADH + H+
-
Helicobacter aurati glycine + H2O + NAD+
-
r
1.4.1.1 L-alanine + H2O + NAD+
-
Helicobacter aurati pyruvate + NH3 + NADH + H+
-
r
1.4.1.1 additional information isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids Helicobacter aurati ?
-
-
1.4.1.1 additional information L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively Helicobacter aurati ?
-
-
1.4.1.1 oxaloacetate + NH3 + NADH + H+
-
Helicobacter aurati L-aspartate + H2O + NAD+
-
r
1.4.1.1 pyruvate + NH3 + NADH + H+
-
Helicobacter aurati L-alanine + H2O + NAD+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.4.1.1 ADH
-
Helicobacter aurati
1.4.1.1 ALD
-
Helicobacter aurati
1.4.1.1 CQA66_00465
-
Helicobacter aurati
1.4.1.1 HAADH1
-
Helicobacter aurati
1.4.1.1 HAADH2
-
Helicobacter aurati

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.1.1 55
-
recombinant enzyme Helicobacter aurati

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.1 8
-
deamination reaction, recombinant enzyme Helicobacter aurati
1.4.1.1 9
-
amination reaction, recombinant enzyme Helicobacter aurati

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.1.1 additional information
-
the enzyme reaches maximum activity in the oxidation reaction at pH 9.0, but almost completely loses its activity at pH 10.0 Helicobacter aurati

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.1.1 8
-
most stable pH for isozyme HADDH1 is pH 8.0 Helicobacter aurati

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.1 additional information the enzyme shows no activity with NADP+ and NADPH as cofactors Helicobacter aurati
1.4.1.1 NAD+
-
Helicobacter aurati
1.4.1.1 NADH
-
Helicobacter aurati

General Information

EC Number General Information Comment Organism
1.4.1.1 evolution sequence comparisons and phylogenetic analysis Helicobacter aurati
1.4.1.1 evolution sequence comparisons and phylogenetic analysis indicate that enzyme HAADH1 is a distinct type of alanine dehydrogenase Helicobacter aurati

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.4.1.1 8.1
-
L-alanine recombinant enzyme, pH 8.0, 55°C Helicobacter aurati
1.4.1.1 364
-
pyruvate recombinant enzyme, pH 9.0, 55°C Helicobacter aurati