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Literature summary for 2.6.1.B21 extracted from

  • Han, S.; Shin, J.
    One-pot preparation of D-amino acids through biocatalytic deracemization using alanine dehydrogenase and omega-transaminase (2018), Catal. Lett., 148, 3678-3684 .
No PubMed abstract available

Application

Application Comment Organism
synthesis in another reaction for deracemization using enantiocomplementary transaminases, the oxidative deamination step is carried out by alpha-transaminase such as branched-chain transaminase (EC 2.6.1.42) and D-amino acid transaminase (EC 2.6.1.21). It is notable that substitution of alpha-transaminase with alanine dehydrogenase in the deracemization method for production of D-amino acids using L-alanine dehydrogenase (AlaDH), D-selective omega-transaminase (omega-TA) ARTAmut, and NADH oxidase (NOX) eliminates the need for an expensive 2-oxoacid cosubstrate. Feasibility of the stereoinversion reaction is dependent on enzyme activities of AlaDH and onega-TA for L-amino acids and its keto acids, respectively. ARTAmut substrate specificity allows various oxoacids as substrates Arthrobacter sp.

Cloned(Commentary)

Cloned (Comment) Organism
construction of the pET28a vector carrying a codon-optimized gene of an engineered D-selective omega-transaminase (omega-TA) ARTAmut from Arthrobacter sp. (ARTAmut), recombinant expression of His-tagged omega-TA in Escherichia coli strain BL21(DE3) Arthrobacter sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-alpha-methylbenzylamine + pyruvate Arthrobacter sp.
-
acetophenone + L-alanine
-
r

Organism

Organism UniProt Comment Textmining
Arthrobacter sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged ARTA mut from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and desalting gel filtration Arthrobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-alpha-methylbenzylamine + pyruvate
-
Arthrobacter sp. acetophenone + L-alanine
-
r
(R)-alpha-methylbenzylamine + pyruvate isopropylamine is one of the preferred amino donors for omega-TA Arthrobacter sp. acetophenone + L-alanine
-
r
2-oxo-4-hydroxybutyrate + isopropylamine low activity, 6% activity compared to pyruvate Arthrobacter sp. D-homoserine + acetone
-
r
2-oxo-hexanoate + isopropylamine low activity, 2% activity compared to pyruvate Arthrobacter sp. D-norleucine + acetone
-
r
2-oxobutyrate + isopropylamine 33% activity compared to pyruvate Arthrobacter sp. D-2-aminobutyrate + acetone
-
r
2-oxovalerate + isopropylamine low activity, 2% activity with 2b compared to pyruvate Arthrobacter sp. D-2-amino-pentanoate + acetone
-
r
additional information developed of a deracemization method for production of D-amino acids using L-alanine dehydrogenase (AlaDH), D-selective omega-transaminase (omega-TA) ARTAmut, and NADH oxidase (NOX). Unwanted L-amino acid in the racemic mixture is converted to a D-form after two consecutive reactions catalyzed by AlaDH and ARTA mut, leading to complete deracemization or enantioenrichment depending on the substrate specificity of the two enzymes, reaction cascade and method evaluation, overview Arthrobacter sp. ?
-
-
pyruvate + isopropylamine
-
Arthrobacter sp. D-alanine + acetone
-
r

Subunits

Subunits Comment Organism
homodimer
-
Arthrobacter sp.

Synonyms

Synonyms Comment Organism
ARTAmut
-
Arthrobacter sp.
D-selective omega-TA
-
Arthrobacter sp.
omega-TA
-
Arthrobacter sp.
omega-transaminase
-
Arthrobacter sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Arthrobacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Arthrobacter sp.

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP, dependent on Arthrobacter sp.

General Information

General Information Comment Organism
evolution the enzyme is a PLP fold type IV transaminase. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme. PLP fold type IV transaminases include branched-chain amino acid transaminases (BCATs), D-amino acid transaminases, and (R)-amine:pyruvate transaminases. A small substrate binding pocket which is a general property for all the omega-TAs known to date Arthrobacter sp.