rennin (but this should be avoided since it leads to confusion withrenin)
The structure and function of acid proteases. III. Isolation and characterization of the active-site peptides from bovine rennin.
Alteration of catalytic properties of chymosin by site-directed mutagenesis.
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT.
Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin.
Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis.
The three-dimensional structure of recombinant bovine chymosin at 2.3 A resolution.
X-ray structural studies of mammalian aspartic proteinases.
Functional implications of the three-dimensional structure of bovine chymosin.
X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin.
Can enzymes adopt a self-inhibited form? Results of x-ray crystallographic studies of chymosin.
Functional implication of disulfide bond, Cys250 -Cys283, in bovine chymosin.
Domain flexibility in aspartic proteinases.
Protein engineering of surface loops: preliminary X-ray analysis of the CHY155-165RHI mutant.
Restrained molecular dynamics study of the interaction between bovine kappa-casein peptide 98-111 and bovine chymosin and porcine pepsin.
Post X-ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of kappa-casein.
Protein engineering loops in aspartic proteinases: site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin.
Functional implications of disulfide bond, Cys45-Cys50, in recombinant prochymosin.
Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosin.
Protein engineering aspartic proteinases. Site-directed mutagenesis, biochemical characterisation, and X-ray analysis of chymosins with substituted single amino acid substitutions and loop replacements.
Post X-ray crystallographic studies of chymosin specificity. The role of histidine-proline cluster of kappa-casein in catalytic reactions.
Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin.
A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure.
Functional implications of disulfide bond, Cys206-Cys210, in recombinant prochymosin (chymosin).
A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin.
Role of S'1 loop residues in the substrate specificities of pepsin A and chymosin.
This enzyme belongs to the peptidase family-A1. This enzyme has got a catalytic dyad, composed of two aspartic acid residues, which are conserved among other aspartate proteases such as pepsin (D00436 in EzCatDB). Thus, its catalytic mechanism must be similar to those.