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Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]
Xaa-Pro dipeptidase, also known as prolidase, is an enzyme that in humans is encoded by the PEPD gene. [5] [6] [7] Prolidase is an enzyme in humans that plays a crucial role in protein metabolism and collagen recycling through the catalysis of the rate-limiting step in these chemical reactions. [8]
In molecular biology, the Signal Peptide Peptidase (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs).
They also participate in specific functions like the cleavage of N-terminal (beginning) methionine from newly synthesized peptide chains (methionine aminopeptidases), stabilization of ColE1-based multicopy plasmids (e.g. aminopeptidase A), and the cleavage of N-terminal pyroglutamate (e.g. pyroglutamyl aminopeptidase. [13]
The eukaryotic signal peptidase is an integral membrane protein complex. The first subunit, which was identified by yeast genetics is Sec11, a 17 kDa membrane protein that is associated with three subunits termed Spc3p (21 kDa), Spc2p (18 kDa) and Spc1p (11 kDa).
The nuclear-gene encoded mitochondrial matrix LON peptidase 1 (LONP1), originally thought to be responsible for protein quality control (PQC) by degrading unfolded or misfolded proteins, has several essential functions like proteolytic activity, chaperone activity and mitochondrial DNA (mtDNA) regulation.
Mitochondrial processing peptidase is an enzyme complex found in mitochondria which cleaves signal sequences from mitochondrial proteins. In humans this complex is composed of two subunits encoded by the genes PMPCA , and PMPCB .
Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. The animal pepsin-like endopeptidase propeptides form a distinct family of propeptides, which contain a conserved motif approximately 30 residues long.