A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin

Author:

Francky Andrej,Francky Bojana Mozetič,Štrukelj Borut,Gruden Kristina,Ritonja Anka,Križaj Igor,Kregar Igor,Pain Roger H.,Pungerčar Jože

Publisher

Wiley

Subject

Biochemistry

Reference32 articles.

1. Chymosin: a short review on foetal and neonatal gastric proteases;Foltmann;Scand. J. Clin. Lab. Invest.,1992

2. The tryptic peptide with the renin-sensitive linkage of cow’s κ-casein;Jolles;Biochim. Biophys. Acta,1968

3. Investigations on the activation of bovine prochymosin;Pedersen;Eur. J. Biochem.,1979

4. Structure and function of proparts in zymogens for aspartic proteinases;Foltmann;Biol. Chem. Hoppe-Seyler,1988

5. Refined structure of porcine pepsinogen at 1.8 Å resolution;Sielecki;J. Mol. Biol.,1991

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1. The propeptide sequence assists the correct folding required for the enzymatic activity of cocoonase;Biochemical and Biophysical Research Communications;2022-10

2. Foldase and inhibitor functionalities of the pepsinogen prosegment are encoded within discrete segments of the 44 residue domain;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2015-10

3. Chymosin;Handbook of Proteolytic Enzymes;2013

4. Cloning, Expression, Purification and Refolding of Caprine Prochymosin;Food Biotechnology;2012-04

5. Recombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2009-12

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