Multiple implications of an active site phenylalanine in the catalysis of aryl-alcohol oxidase.

ABSTRACT: Aryl-alcohol oxidase (AAO) has demonstrated to be an enzyme with a bright future ahead due to its biotechnological potential in deracemisation of chiral compounds, production of bioplastic precursors and other reactions of interest. Expanding our understanding on the AAO reaction mechanisms, through the investigation of its structure-function relationships, is crucial for its exploitation as an industrial biocatalyst. In this regard, previous computational studies suggested an active role for AAO Phe397 at the active-site entrance. This residue is located in a loop that partially covers the access to the cofactor forming a bottleneck together with two other aromatic residues. Kinetic and affinity spectroscopic studies, complemented with computational simulations using the recently develope

SUBMITTER: Carro J 

PROVIDER: S-EPMC5970180 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature