Ontology highlight
ABSTRACT:
SUBMITTER: Wu MH
PROVIDER: S-EPMC6070645 | biostudies-literature | 2018 Aug
REPOSITORIES: biostudies-literature
Wu Meng-Hsuan MH Lee Cheng-Chung CC Hsiao An-Shan AS Yu Su-May SM Wang Andrew H-J AH Ho Tuan-Hua David TD
FEBS open bio 20180703 8
A high-efficiency laccase, DLac, was isolated from <i>Cerrena</i> sp. RSD1. The kinetic studies indicate that DLac is a diffusion-limited enzyme. The crystal structure of DLac was determined to atomic resolution, and its overall structure shares high homology to monomeric laccases, but displays unique substrate-binding loops from those in other laccases. The substrate-binding residues with small side chain and the short substrate-binding loop IV broaden the substrate-binding cavity and may facil ...[more]