8V16
Esterase with a monomeric cooperative, hysteresis or allokairy
Summary for 8V16
| Entry DOI | 10.2210/pdb8v16/pdb |
| Descriptor | Esterase 1, GLYCEROL (3 entities in total) |
| Functional Keywords | esterase, hysteresis/allokairy, metagenomic, alpha/beta-hydrolases, hydrolase |
| Biological source | uncultured proteobacterium |
| Total number of polymer chains | 4 |
| Total formula weight | 120282.79 |
| Authors | |
| Primary citation | Vinces, T.C.,de Souza, A.S.,Carvalho, C.F.,Visnardi, A.B.,Teixeira, R.D.,Llontop, E.E.,Bismara, B.A.P.,Vicente, E.J.,Pereira, J.O.,de Souza, R.F.,Yonamine, M.,Marana, S.R.,Farah, C.S.,Guzzo, C.R. Monomeric Esterase: Insights into Cooperative Behavior, Hysteresis/Allokairy. Biochemistry, 63:1178-1193, 2024 Cited by PubMed Abstract: Herein, we present a novel esterase enzyme, Ade1, isolated from a metagenomic library of Amazonian dark earths soils, demonstrating its broad substrate promiscuity by hydrolyzing ester bonds linked to aliphatic groups. The three-dimensional structure of the enzyme was solved in the presence and absence of substrate (tributyrin), revealing its classification within the α/β-hydrolase superfamily. Despite being a monomeric enzyme, enzymatic assays reveal a cooperative behavior with a sigmoidal profile (initial velocities vs substrate concentrations). Our investigation brings to light the allokairy/hysteresis behavior of Ade1, as evidenced by a transient burst profile during the hydrolysis of substrates such as -nitrophenyl butyrate and -nitrophenyl octanoate. Crystal structures of Ade1, coupled with molecular dynamics simulations, unveil the existence of multiple conformational structures within a single molecular state (E̅). Notably, substrate binding induces a loop closure that traps the substrate in the catalytic site. Upon product release, the cap domain opens simultaneously with structural changes, transitioning the enzyme to a new molecular state (E̅). This study advances our understanding of hysteresis/allokairy mechanisms, a temporal regulation that appears more pervasive than previously acknowledged and extends its presence to metabolic enzymes. These findings also hold potential implications for addressing human diseases associated with metabolic dysregulation. PubMed: 38669355DOI: 10.1021/acs.biochem.3c00668 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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