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Properties of bacterial and archaeal branched-chain amino acid aminotransferases

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Abstract

Branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. BCATs are the key enzymes of BCAA metab- olism in all organisms. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyri- doxal 5′-phosphate (PLP). BCATs differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is imple- mented via the “lock and key” mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate α-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine for- mation in BCAT catalysis. In this review, the structure-function features and the substrate specificity of bacterial and archaeal BCATs are analyzed. These BCATs differ from eukaryotic ones in the wide substrate specificity, optimal tempera- ture, and reactivity toward pyruvate as the second substrate. The prospects of biotechnological application of BCATs in stereoselective synthesis are discussed.

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Abbreviations

AAT:

aspartate aminotransferase

BCAA:

branched-chain amino acid

BCAT:

branched-chain amino acid aminotransferase

DAAT:

D-amino acid transaminase

eBCAT:

BCAT from E. coli

GDH:

glutamate dehydrogenase

MtBCAT:

BCAT from Mycobacterium tuberculosis

PLP:

pyri-doxal 5’-phosphate

PMP:

pyridoxamine 5’-phosphate

TA:

transaminase

Ts-BcAT:

BCAT from Thermococcus sp. CKU-1

TUZN1299:

BCAT from Thermoproteus uzoniensis

VMUT0738:

BCAT from Vulcanisaeta moutnovskia

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Authors and Affiliations

  1. Bach Institute of Biochemistry, The Federal Research Centre “Fundamentals of Biotechnology”, Russian Academy of Sciences, 119071, Moscow, Russia

    E. Yu. Bezsudnova, K. M. Boyko & V. O. Popov

  2. National Research Center “Kurchatov Institute”, 123098, Moscow, Russia

    K. M. Boyko & V. O. Popov

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  1. E. Yu. Bezsudnova
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  2. K. M. Boyko
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  3. V. O. Popov
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Correspondence to E. Yu. Bezsudnova.

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Original Russian Text © E. Yu. Bezsudnova, K. M. Boyko, V. O. Popov, 2017, published in Uspekhi Biologicheskoi Khimii, 2017, Vol. 57, pp. 33-70.

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Bezsudnova, E.Y., Boyko, K.M. & Popov, V.O. Properties of bacterial and archaeal branched-chain amino acid aminotransferases. Biochemistry Moscow 82, 1572–1591 (2017). https://doi.org/10.1134/S0006297917130028

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  • DOI: https://doi.org/10.1134/S0006297917130028

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