oxidized polyvinyl alcohol hydrolase in Stenotrophomonas rhizophila QL-P4
Comparative genomic analysis identified BAY15_0160 as a candidate OPH homolog exhibiting the characteristic a/ß-hydrolase superfamily folding pattern. Structural interrogation revealed that the catalytic domain maintains the essential architecture characteristic of hydrolases, featuring the lipase-specific Gly-X-Ser-X-Gly motif, as identified through sequence alignment. This structural evidence provides mechanistic validation that BAY15_0160 functions as a ß-diketone lyase by specifically cleaving C-C bonds in oxidized PVA substrates