The complete amino acid sequence of prochymosin.
- 1 June 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (6) , 2321-2324
- https://doi.org/10.1073/pnas.74.6.2321
Abstract
The total sequence of 365 amino acid residues in bovine prochymosin is presented. Alignment with the amino acid sequence of porcine pepsinogen shows that 204 amino acid residues are common to the 2 zymogens. Further comparison and alignment with the amino acid sequence of penicillopepsin shows that 66 residues are located at identical positions in all 3 proteases. The 3 enzymes belong to a large group of proteases with 2 aspartate residues in the active center. This group forms a family derived from one common ancestor.This publication has 34 references indexed in Scilit:
- The crystal structure at 5.5Å resolution of an acid-protease from Rhizopus chinensisBiochemical and Biophysical Research Communications, 1976
- Bovine pepsin: The sequence of the first 65 amino acid residues (completing the sequence of the first 110 residues of bovine pepsinogen)FEBS Letters, 1975
- The amino terminal sequences of acid proteases - human pepsin and gastricsin and the protease of Rhizopus chinensisBiochemical and Biophysical Research Communications, 1975
- Definitive evidence for similarity in the active site of renin and acidic proteaseBiochemical and Biophysical Research Communications, 1974
- The amino acid sequence of a hitherto unobserved segment from porcine pepsinogen preceeding the N‐terminus of pepsinFEBS Letters, 1973
- The amino acid sequence of the first 61 residues of chymosin (rennin EC 3.4.4.3)FEBS Letters, 1973
- The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergilius awamori — An analog of penicillopepsin and pepsinBiochemical and Biophysical Research Communications, 1972
- Inhibition of cathepsin D by diazoacetylnorleucine methyl esterFEBS Letters, 1970
- On the mechanism of action of pepsinPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- The sequence around an active‐site aspartyl residue in pepsinFEBS Letters, 1968