Carboxylesterase 5 (CES5), also called cauxin or CES7, is a member of carboxylesterases family which plays an important role in the hydrolysis of ester and amide bonds. Carboxylesterase is a type of enzyme that capable of hydrolyzing a variety of carboxylic acid esters and it's widely distributed in cells especially in mammalian liver. CES5 is with broad substrate specificity ranging from small molecule esters to longchain fatty acid esters and thioesters. It has been previously reported CES5 was in high concentrations in the urine (cauxin) of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for CES5 may include regulating urinary levels of male cat pheromones, catalyzing lipid transfer reactions within mammalian male reproductive fluids, and protecting neural tissue from drugs and xenobiotics.
Carboxylesterase belongs to the class of serine hydrolases family which includes Chymotrypsin and Acetylcholinesterase. Carboxylesterase is involved in the chemical reaction, exerting its role in catalyzing the carboxylic ester and water to convert to an alcohol and a carboxylate. Carboxylesterase is a type of enzyme that capable of hydrolyzing a variety of carboxylic acid esters and it's widely distributed in cells especially in mammalian liver. Carboxylesterase 5 (CES5), also known as cauxin or CES7, is one of CES enzyme families exerting role in catalyzing hydrolytic and transesterfication reactions with broad substrat specifity. CES5 is reported in high concentrations in the urine of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for carboxylesterase 5 may include regulating urinary levels of cat pheromone, catalyzing lipid transfer reactions within mammalian male reproductive fluids, and protecting neural tissue from drugs and xenobiotics.
Carboxypeptidase A1 （CPA1）is secreted as a pancreatic procarboxypeptidase, and cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group, with the preference of residues with aromatic or branched aliphatic side chains. CPA1 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition. Three different forms of human pancreatic procarboxypeptidase A have been isolated.
Carboxypeptidase B1, also well known as pancreatic procarboxypeptidase B (PCPB), is a highly pancreas -specific protein (PASP), and has been identified previously as a serum marker for acute pancreatitis and pancreatic graft rejection. As the prototype for those human exopeptidases that cleave off basic C-terminal residues, CPB1 specifically cleaves the C-terminal Arg and Lys residues with a preference for Arg. The B1 and B2 forms of procarboxypeptidase B differ from each other mainly in isoelectric point.The deduced amino acid sequence of PCPB predicts a 416-amino acid preproenzyme consisting of a 15-aa signal peptide, a 95-aa activation peptide and a 307-aa mature chain. The secreted PCPB zymogen is converted to enzymatically active CPB1 by limited proteolysis by trypsin.
Carboxypeptidase B2, also known as Carboxypeptidase U, Thrombin-activable fibrinolysis inhibitor, Plasma carboxypeptidase B, CPB2, is a secreted protein which belongs to the peptidase M14 family. Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). CPB2 is activated by thrombin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. CPB2 is synthesized by the liver and circulates in the plasma as a plasminogen-bound zymogen. When it is activated by proteolysis at residue Arg92 by the thrombin / thrombomodulin complex. CPB2 cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. CPB2 exhibits carboxypeptidase activity and activated CPB2 reduces fibrinolysis by removing the fibrin C-terminal residues that are important for the binding and activation of plasminogen.
Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the carboxypeptidases family. These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the surface of specialized cells and tissues in the human body. CPM in the brain appears to be membrane-bound via a phosphatidylinositol glycan anchor. CPM is widely distributed in a variety of tissues and cells. The amino acid sequence of CPM indicated that the C-terminal hydrophobic region might be a signal for membrane attachment via a glycosylphosphatidylinositol (GPI) anchor. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions.
Carboxypeptidase M (CPM) belongs to the peptidase M14 family, and exists in cell membrane. The protein binds 1 zinc ion per subunit, and cleavage of C-terminal arginine or lysine residues from polypeptides. CPM specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
Caspase-1, also known as IL-1 beta-converting enzyme (ICE), is an aspartic protease that plays a key role in the inflammatory response and apoptosis. Caspase-1 precursor (about 50kDa) can be cleaved and the active enzyme consists of a complex of two 20 kDa (aa 120-297) and two 10 kDa (aa 317-404) subunits which associate following cleavage of inactive precursors. Caspase-1 is required for proteolytic cleavage of the IL-1 beta precursor to form the active proinflammatory cytokine. Alternate splicing generates several additional Caspase-1 isoforms with deletions in the propeptide regions or also in the mature subunits.
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