carboxypeptidase a造句

• This mechanism ensures that the cells wherein pro-carboxypeptidase A is produced are not themselves digested.
• Classified as a metalloexopeptidase, carboxypeptidase A consists of a single polypeptide chain bound to a zinc ion.
• For example, a drug that treats high blood pressure, Captopril, was designed based on a carboxypeptidase A inhibitor.
• Recent biomedical research on collagenase, enkephlinase, and angiotensin-converting enzyme used carboxypeptidase A for inhibitor synthesis and kinetic testing.
• However, once ligand binds at the active site of carboxypeptidase A, this coordination number can vary from five to six.
• The carboxypeptidase A family can be divided into two subfamilies : carboxypeptidase H ( regulatory ) and carboxypeptidase A ( digestive ).
• The carboxypeptidase A family can be divided into two subfamilies : carboxypeptidase H ( regulatory ) and carboxypeptidase A ( digestive ).
• David Cushman, Miguel Ondetti and colleagues used peptide analogues to study the structure of ACE, using carboxypeptidase A as a model.
• This would yield a coordination number of six for the zinc in the carboxypeptidase A-dipeptide glycyl-L-tyrosine complex.
• This property of carboxypeptidase A led to the first clause of Daniel E . Koshland, Jr .  s  induced fit hypothesis.
• Several studies have been conducted exploring the details of the bond between carboxypeptidase A and substrate and how this affects the rate of hydrolysis.
• According to their substrate specificity, these enzymes are referred to as carboxypeptidase A ( cleaving aliphatic residues ) or carboxypeptidase B ( cleaving basic amino residues ).
• Leucine aminopeptidase, ( left ) a little like carboxypeptidase A, chops off certain amino acids one-by-one from one end of a protein or peptide.
• Carboxypeptidase A and the target enzyme of Captopril, angiotensin-converting enzyme, have very similar structures, as they both contain a zinc ion within the active site.
• This allowed for a potent carboxypeptidase A inhibitor to be used to inhibit the enzyme and, thus, lower blood pressure through the renin-angiotensin-aldosterone system.
• In the case of pancreatic carboxypeptidase A, the inactive zymogen form-pro-carboxypeptidase A-is converted to its active form-carboxypeptidase A-by the enzyme trypsin.
• In the case of pancreatic carboxypeptidase A, the inactive zymogen form-pro-carboxypeptidase A-is converted to its active form-carboxypeptidase A-by the enzyme trypsin.
• In the case of pancreatic carboxypeptidase A, the inactive zymogen form-pro-carboxypeptidase A-is converted to its active form-carboxypeptidase A-by the enzyme trypsin.
• There are two proposed mechanisms for the catalytic function of carboxypeptidase A . The first is a nucleophilic pathway involving a covalent acyl enzyme intermediate containing active site base Glu-270.
• Carboxypeptidase A is produced in the pancreas and is crucial to many processes in the human body to include digestion, post-translational modification of proteins, blood clotting, and reproduction.