Elucidation of the Molecular Mechanism of Bovine Milk γ-Glutamyltransferase Catalyzed Formation of γ-Glutamyl-Valyl-Glycine
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Elucidation of the Molecular Mechanism of Bovine Milk γ-Glutamyltransferase Catalyzed Formation of γ-Glutamyl-Valyl-Glycine. / Cao, Lichuang; Hunt, Cameron J.; Lin, Shang; Meyer, Anne S.; Li, Qian; Lametsch, René.
In: Journal of Agricultural and Food Chemistry, Vol. 71, No. 5, 2023, p. 2455-2463.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Elucidation of the Molecular Mechanism of Bovine Milk γ-Glutamyltransferase Catalyzed Formation of γ-Glutamyl-Valyl-Glycine
AU - Cao, Lichuang
AU - Hunt, Cameron J.
AU - Lin, Shang
AU - Meyer, Anne S.
AU - Li, Qian
AU - Lametsch, René
N1 - Publisher Copyright: © 2023 American Chemical Society.
PY - 2023
Y1 - 2023
N2 - γ-Glu-Val-Gly (γ-EVG) is a potent kokumi peptide that can be synthesized through the transpeptidase reaction catalyzed by γ-glutamyl transferase from bovine milk (BoGGT). To explore the molecular mechanism between BoGGT and l-glutamine, γ-glutamyl peptides were generated through the transpeptidase reaction catalyzed by BoGGT at various reaction conditions. Quantitation of γ-glutamyl peptides, structure prediction of BoGGT, molecular docking, and molecular dynamic simulations were performed. Membrane-free BoGGT had a higher transpeptidase activity with Val-Gly as an acceptor than membrane BoGGT. The suitable conditions for γ-EVG production using BoGGT were 100 mM Val-Gly, 20 mM Gln, 1.2 U/mL BoGGT, pH 8.5, and 37 °C, and 13.1 mM γ-EVG was produced. The hydrogen bonds are mainly formed between residues from the light subunit of BoGGT (Thr380, Thr398, Ser450, Ser451, Met452, and Gly473) and the l-glutamine donor. NaCl might inhibit the transpeptidase activity by destroying the hydrogen bonds between BoGGT and l-glutamine, thereby increasing the distance between the hydroxyl oxygen atom on Thr380 of BoGGT and the amide carbon atom on l-glutamine.
AB - γ-Glu-Val-Gly (γ-EVG) is a potent kokumi peptide that can be synthesized through the transpeptidase reaction catalyzed by γ-glutamyl transferase from bovine milk (BoGGT). To explore the molecular mechanism between BoGGT and l-glutamine, γ-glutamyl peptides were generated through the transpeptidase reaction catalyzed by BoGGT at various reaction conditions. Quantitation of γ-glutamyl peptides, structure prediction of BoGGT, molecular docking, and molecular dynamic simulations were performed. Membrane-free BoGGT had a higher transpeptidase activity with Val-Gly as an acceptor than membrane BoGGT. The suitable conditions for γ-EVG production using BoGGT were 100 mM Val-Gly, 20 mM Gln, 1.2 U/mL BoGGT, pH 8.5, and 37 °C, and 13.1 mM γ-EVG was produced. The hydrogen bonds are mainly formed between residues from the light subunit of BoGGT (Thr380, Thr398, Ser450, Ser451, Met452, and Gly473) and the l-glutamine donor. NaCl might inhibit the transpeptidase activity by destroying the hydrogen bonds between BoGGT and l-glutamine, thereby increasing the distance between the hydroxyl oxygen atom on Thr380 of BoGGT and the amide carbon atom on l-glutamine.
KW - bovine milk
KW - inhibition mechanism
KW - molecular dynamics
KW - γ-Glu-Val-Gly
KW - γ-glutamyl transferase
U2 - 10.1021/acs.jafc.2c08386
DO - 10.1021/acs.jafc.2c08386
M3 - Journal article
C2 - 36706241
AN - SCOPUS:85147168654
VL - 71
SP - 2455
EP - 2463
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 5
ER -
ID: 339887107