Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber.

ABSTRACT: Latex clearing proteins (Lcps) are rubber oxygenases that catalyse the extracellular cleavage of poly (cis-1,4-isoprene) by Gram-positive rubber degrading bacteria. Lcp of Streptomyces sp. K30 (Lcp_K30) is a b-type cytochrome and acts as an endo-type dioxygenase producing C₂₀ and higher oligo-isoprenoids that differ in the number of isoprene units but have the same terminal functions, CHO-CH₂- and -CH₂-COCH₃. Our analysis of the Lcp_K30 structure revealed a 3/3 globin fold with additional domains at the N- and C-termini and similarities to globin-coupled sensor proteins. The haem group of Lcp_K30 is ligated to the polypeptide by a proximal histidine (His198) and by a lysine residue (Lys167) as the distal axial ligand

SUBMITTER: Ilcu L 

PROVIDER: S-EPMC5522427 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature