Xs. Puente et al., STRUCTURAL CHARACTERIZATION AND CHROMOSOMAL LOCALIZATION OF THE GENE ENCODING HUMAN BIPHENYL HYDROLASE-RELATED PROTEIN (BPHL), Genomics (San Diego, Calif.), 51(3), 1998, pp. 459-462
The gene encoding human biphenyl hydrolase-related protein (Bph-rp), a
serine hydrolase with sequence similarity to prokaryotic enzymes invo
lved 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 intr
ons differ from those reported for the genes encoding other serine hyd
rolases with sequence similarity to Bph rp, indicating that these gene
s are distantly related. Nucleotide sequence analysis of the 5'-flanki
ng 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 hydr
olases mapped to date. (C) 1998 Academic Press