Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
Catalysis of the hydrolysis of C-terminal amino acid residues from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
J. Biol. Chem. 265, 11306-11311 (1990)[PubMed:1972707]
Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. By using human prolidase cDNA as a probe, a chromosomal gene related to prolidase was isolated from human gene libraries. The human prolidase gene is over 130 kilobases long and is split into 15 exons. All of the splice donor and acceptor sites conform to the GT/AG rule. The transcription initiation site was determined by nuclease S1 mapping and primer extension and was located 131 bases upstream from the initiation codon. A "CAAT" box-like sequence was present 67 bases upstream from the cap site, but there was no "TATA" box-like sequence. There were seven sets of sequences resembling the transcription factor Sp1 binding sites. Four were upstream from the cap site, and three were downstream. We also analyzed findings in patients with prolidase deficiency with respect to major gene re-arrangement. Several hundred base deletions, including the 14th exon, were identified. Knowledge of the gene structure of human prolidase will facilitate further studies on the expression and regulation of this gene and provide necessary information for analyses of mutations in patients with this deficiency.
J. Biol. Chem. 265, 11306-11311 (1990)[PubMed:1972707]
Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. By using human prolidase cDNA as a probe, a chromosomal gene related to prolidase was isolated from human gene libraries. The human prolidase gene is over 130 kilobases long and is split into 15 exons. All of the splice donor and acceptor sites conform to the GT/AG rule. The transcription initiation site was determined by nuclease S1 mapping and primer extension and was located 131 bases upstream from the initiation codon. A "CAAT" box-like sequence was present 67 bases upstream from the cap site, but there was no "TATA" box-like sequence. There were seven sets of sequences resembling the transcription factor Sp1 binding sites. Four were upstream from the cap site, and three were downstream. We also analyzed findings in patients with prolidase deficiency with respect to major gene re-arrangement. Several hundred base deletions, including the 14th exon, were identified. Knowledge of the gene structure of human prolidase will facilitate further studies on the expression and regulation of this gene and provide necessary information for analyses of mutations in patients with this deficiency.
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
Enzyme which catalyzes hydrolysis reaction, i.e. the addition of the hydrogen and hydroxyl ions of water to a molecule with its consequent splitting into two or more simpler molecules.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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