The “Active Site” of Bovine Pancreatic Carboxypeptidase A
نویسندگان
چکیده
منابع مشابه
Binding of ligands to the active site of carboxypeptidase A.
We compare the detailed binding modes of the 39-amino acid inhibitor from potatoes, glycyl-L-tyrosine, the ester analogue CH3OC6H4(CO)CH2CH(CO2(-))C6H5, and indole acetate to the exopeptidase carboxypeptidase A (EC 3.4.17.1). In the potato inhibitor, cleavage of the COOH-terminal glycine-39 leaves a new carboxylate anion of valine-38 having one oxygen on zinc and the other as a receptor of a hy...
متن کاملPutative secondary active site of bovine pancreatic deoxyribonuclease I.
Previous structural studies based on the co-crystal of a complex between bovine pancreatic deoxyribonuclease I (bpDNase I) and a double-stranded DNA octamer d(GCGATCGC)(2) have suggested the presence of a putative secondary active site near Ser43. In our present study, several crucial amino acid residues postulated in this putative secondary active site, including Thr14, Ser43, and His44 were s...
متن کاملpK values for active site residues of carboxypeptidase A.
The phenolic group of active site residue Tyr-248 in carboxypeptidase A has a pKa value of 10.06, as determined from the pH dependence of its rate of nitration by tetranitromethane. The decrease in enzyme activity (kcat/Km) in alkaline solution, characterized by a pKa value of approximately 9.0 (for cobalt carboxypeptidase A), is associated with the protonation state of an imidazole ligand of t...
متن کاملAlkylation of a histidine residue at the active site of bovine pancreatic deoxyribonuclease.
In the study of reactions designed to identify the amino acid residues most directly involved in the catalytic function of pancreatic deoxyribonuclease, the enzyme was tist treated with iodoacetate under conditions similar to those which are effective in alkylating essential histidine residues in pancreatic ribonuclease; no inactivation of DNase occurred although some reagent was incorporated. ...
متن کاملThe active site and mechanism of action of bovine pancreatic ribonuclease. 7. The catalytic mechanism.
The previous papers in this series (Crook, Mathias d& Rabin, 1960a, b; Herries, Mathias & Rabin, 1962; Findlay, Mathias & Rabin, 1962a, b; Ross, Mathias & Rabin, 1962) provide evidence that the catalytic site of ribonuclease contains two imidazole groups; one of these is required in the acid form and the other in the base form. For the hydrolysis of cytidine 2',3'-phosphate, the shifts in the p...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1960
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)64586-7