Enzyme catalysis prior to aromatic residues: Reverse engineering of a dephospho-CoA kinase.

ABSTRACT: The wide variety of protein structures and functions results from the diverse properties of the 20 canonical amino acids. The generally accepted hypothesis is that early protein evolution was associated with enrichment of a primordial alphabet, thereby enabling increased protein catalytic efficiencies and functional diversification. Aromatic amino acids were likely among the last additions to genetic code. The main objective of this study was to test whether enzyme catalysis can occur without the aromatic residues (aromatics) by studying the structure and function of dephospho-CoA kinase (DPCK) following aromatic residue depletion. We designed two variants of a putative DPCK from Aquifex aeolicus by substituting (a) Tyr, Phe and Trp or (b) all aromatics (including His). Their structural ch

SUBMITTER: Makarov M 

PROVIDER: S-EPMC8040869 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature