The gene encoding human biphenyl hydrolase-related protein (Bph-rp), a serine hydrolase with sequence similarity to prokaryotic enzymes involved in the degradation of polychlorinated biphenyls, has been cloned and its overall organization established. The gene, whose HGM-approved nomenclature is BPHL, spans more than 30 kb and is composed of eight exons and seven introns. The number and distribution of exons and introns differ from those reported for the genes encoding other serine hydrolases with sequence similarity to Bph-rp, indicating that these genes are distantly related. Nucleotide sequence analysis of the 5'-flanking region of BPHL revealed a high GC content, a ratio CpG/GpC close to unity, and the absence of consensus transcriptional sequences such as a TATA box or a CCAAT box. Chromosomal localization of BPHL revealed that it maps to chromosome 6p25, a unique location for all serine hydrolases mapped to date.
Copyright 1998 Academic Press.