Abstract
Human carboxypeptidase N is a 280-kDa tetrameric enzyme consisting of two 83-kDa regulatory subunits and two catalytic 50-kDa subunits. The 83-kDa subunit is a member of the leucine-rich repeat family of proteins and has been localized to chromosome 8p22–p23. The 50-kDa subunit is a member of the regulatory B-type carboxypeptidase family, which includes carboxypeptidases M, E/H, AEBP1, and a newly described member, carboxypeptidase D, which has three tandem active site domains. The human genes for carboxypeptidase D (HGMW-approved symbol CPD) and the 50-kDa subunit of carboxypeptidase N (HGMW-approved symbol CPN1) were localized to chromosomes 17 and 10, respectively, using the polymerase chain reaction with gene-specific primers and DNAs derived from somatic cell hybrids. The carboxypeptidase D gene was further localized to the centromeric region 17p11.1–q11.1/11.2 by use of a regional mapping panel derived from somatic cell hybrids containing different portions of chromosome 17.
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