Structure-function analyses of a PL24 family ulvan lyase reveal key features and suggest its catalytic mechanism.

ABSTRACT: Ulvan is a major cell wall component of green algae of the genus Ulva, and some marine bacteria encode enzymes that can degrade this polysaccharide. The first ulvan-degrading lyases have been recently characterized, and several putative ulvan lyases have been recombinantly expressed, confirmed as ulvan lyases, and partially characterized. Two families of ulvan-degrading lyases, PL24 and PL25, have recently been established. The PL24 lyase LOR_107 from the bacterial Alteromonadales sp. strain LOR degrades ulvan endolytically, cleaving the bond at the C4 of a glucuronic acid. However, the mechanism and LOR_107 structural features involved are unknown. We present here the crystal structure of LOR_107, representing the first PL24 family structure. We found that LOR_107 adopts a s

SUBMITTER: Ulaganathan T 

PROVIDER: S-EPMC5857984 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature