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Literature summary for 2.6.1.B16 extracted from

  • Manta, B.; Cassimjee, K.; Himo, F.
    Quantum chemical study of dual-substrate recognition in omega-transaminase (2017), ACS Omega, 2, 890-898 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.6.1.B16

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-1-phenylethylamine + pyruvate Chromobacterium violaceum
-
 acetophenone + L-alanine
-
 r

Organism

Organism UniProt Comment Textmining
Chromobacterium violaceum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
pyruvate + (S)-1-phenylethylamine = L-alanine + acetophenone reaction mechanism for the half-transamination of L-alanine to pyruvate in (S)-selective Chromobacterium violaceum omega-transaminase by density functional theory calculations, role of a flexible arginine residue, Arg416, in the dual-substrate recognition. The amine is kinetically favored in the half-transamination of L-alanine/pyruvate, whereas the ketone is kinetically favored in the half-transamination of (S)-1-phenylethylamine/acetophenone. The arginine residue facilitates the dual-substrate recognition by functioning as an arginine switch, where the side chain is positioned inside or outside of the active site depending on the substrate. Arg416 participates in the binding of L-alanine by forming a salt bridge to the carboxylate moiety, whereas the conversion of (S)-1-phenylethylamine is feasible in the absence of Arg416, which here represents the case in which the side chain of Arg416 is positioned outside of the active site. Many PLP-dependent enzymes, including transaminases, require the formation of a so-called internal aldimine (E-PLP), before the main reaction. In this process, the PLP coenzyme becomes covalently bound to an active-site lysine residue as a protonated Schiff base, which constitutes the active form of the enzyme. The transamination reaction consists of two half-transamination equilibria. An amino donor is converted to the corresponding ketone or aldehyde, resulting in the conversion of E-PLP to pyridoxamine-5'-phosphate (PMP). The E-PLP is then regenerated by the reaction of another ketone or aldehyde, which is then converted to an amine Chromobacterium violaceum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-1-phenylethylamine + pyruvate
-
 Chromobacterium violaceum acetophenone + L-alanine
-
 r
(S)-1-phenylethylamine + pyruvate mechanism of the conversion of (S)-1-phenylethylamine to acetophenone, overview Chromobacterium violaceum acetophenone + L-alanine
-
 r

Synonyms

Synonyms Comment Organism
(S)-selective Chromobacterium violaceum omega-transaminase
-
 Chromobacterium violaceum
(S)-selective omega-transaminase
-
 Chromobacterium violaceum
Cv-omegaTA
-
 Chromobacterium violaceum
omega-TA
-
 Chromobacterium violaceum
omega-transaminase
-
 Chromobacterium violaceum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on. Many PLP-dependent enzymes, including transaminases, require the formation of a so-called internal aldimine (E-PLP), before the main reaction. In this process, the PLP coenzyme becomes covalently bound to an active-site lysine residue as a protonated Schiff base, which constitutes the active form of the enzyme. The transamination reaction consists of two half-transamination equilibria. An amino donor is converted to the corresponding ketone or aldehyde, resulting in the conversion of E-PLP to pyridoxamine-5'-phosphate (PMP). The E-PLP is then regenerated by the reaction of another ketone or aldehyde, which is then converted into an amine Chromobacterium violaceum

General Information

General Information Comment Organism
evolution there are two types of TAs, alpha-transaminases, which convert alpha-amino and alpha-keto acids, and omega-transaminases (omegaTAs), which also accept amino and keto acids in which the amino or keto group is in a non-alpha position relative to the carboxyl group, called omega-amino or omega-keto acids, respectively Chromobacterium violaceum
additional information quantum chemical study of dual-substrate recognition in omega-transaminase. The reaction mechanism for the half-transamination of L-alanine to pyruvate in (S)-selective Chromobacterium violaceum omega-transaminase is investigated using density functional theory calculations. The role of a flexible arginine residue, Arg416, in the dual-substrate recognition is revealed using two different active site models, one including this residue and one lacking it. Molecular docking and molecular dynamics simulations, active site modeling, overview. The amino acids that make up the binding site are Phe22, Leu59, Trp60, Phe88', Tyr153, Ile262, and Thr321', as well as Gly230 and Ala231 and the backbone between them Chromobacterium violaceum
physiological function transaminases (TAs) catalyze the reversible interchange of amino and keto groups, by the use of the coenzyme pyridoxal-5'-phosphate (PLP) Chromobacterium violaceum