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Literature summary for 1.4.1.1 extracted from

  • da Silva, E.; Gomez-Vallejo, V.; Llop, J.; Lopez-Gallego, F.
    Structural, kinetic and operational characterization of an immobilized L-aminoacid dehydrogenase (2017), Process Biochem., 57, 80-86 .
No PubMed abstract available
Search for more literature for 1.4.1.1

Application

Application Comment Organism
synthesis the enzyme can be used as heterogeneous biocatalyst for reductive aminations of 2-oxoacids Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information the purified enzyme is immobilized on porous agarose microbeads activated with glyoxyl groups (aliphatic aldehydes). 85% of the offered enzyme is immobilized on these microbeads and the enzyme recovers 45% of its initial reduction amination activity upon the multivalent and irreversible attachment. The immobilized enzyme shows 13fold increased thermostability compared to the soluble enzyme. The optimally immobilized enzyme is also stabilized against acidic pH. The enzyme works as heterogeneous biocatalyst for the synthesis of L-[13N]alanine using pyruvate and [13N]NH4OH obtaining a radiochemical yield of over 95% in 20 minutes. This immobilized enzyme is reused for up to 5 cycles keeping the maximum yield. Immobilization method optimization, overview Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine + H2O + NAD+ Bacillus subtilis
-
 pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+ Bacillus subtilis 168
-
 pyruvate + NH3 + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q08352
-
-
Bacillus subtilis 168 Q08352
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine + H2O + NAD+
-
 Bacillus subtilis pyruvate + NH3 + NADH + H+
-
 r
L-alanine + H2O + NAD+
-
 Bacillus subtilis 168 pyruvate + NH3 + NADH + H+
-
 r

Synonyms

Synonyms Comment Organism
L-AlaDH
-
 Bacillus subtilis
L-AlaDH-Bs
-
 Bacillus subtilis
L-alanine dehydrogenase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 10 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Bacillus subtilis
NADH
-
 Bacillus subtilis

General Information

General Information Comment Organism
physiological function L-alanine dehydrogenase is a NADH-dependent enzyme that catalyzes the reversible reductive amination of pyruvate using ammonia as amine source Bacillus subtilis