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Brian W. Matthews,Benjamin N. Bell,Abigail E. Powell, Carlos Rodriguez,Jennifer R. Cochran,Peter S. Kim, James H. Hurley, Todd P. Silverstein, Matthias Buck, Toshiyuki Shimizu,Xiaoting Tang,Helisa H. Wippel,Juan D. Chavez,James E. Bruce, Jayant B. Udgaonkar,Christina S. Kim,Anne M. Brown,Tijana Z. Grove,Felicia A. Etzkorn, Jayanth R. Banavar,Lorenzo Maso,Matteo Trande,Stefano Liberi,Giulia Moro,Elise Daems,Sara Linciano,Frank Sobott,Sonia Covaceuszach,Alberto Cassetta,Silvano Fasolato,Ligia M. Moretto,Karolien De Wael,Laura Cendron,Alessandro Angelini,Felipe Gonzalez‐Ordenes,Felipe Bravo‐Moraga, Evelin Gonzalez, Leslie Hernandez‐Cabello,Victor Castro‐Fernandez,Rachel Lee,Allen L. Feng,Michael S. Kim,Peter B. Stathopulos, Dan Su

Protein Science（2021）

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摘要

ON THE COVER Enzyme promiscuity is regarded as a key driving force for the evolution of new enzyme functions, and ancestral sequences reconstruction is a powerful tool to investigate the appearance of enzymatic functions in natural enzyme lineages. In this cover image, some techniques used to characterize an ancestral enzyme are represented—an X-ray crystallography pattern and a phylogenetic tree where the ancestral enzyme structure emerges. The substrates tested in the article are shown as sticks; pyridoxal (vitamin B6) in yellow and hydroxymethyl pyrimidine (vitamin B1 intermediate) in orange. See article by GonzalezOrdenes et al., pp. 842–854.

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