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Literature summary extracted from

  • Langholm Jensen, J.; Molgaard, A.; Navarro Poulsen, J.C.; Harboe, M.K.; Simonsen, J.B.; Lorentzen, A.M.; Hjerno, K.; van den Brink, J.M.; Qvist, K.B.; Larsen, S.
    Camel and bovine chymosin: the relationship between their structures and cheese-making properties (2013), Acta Crystallogr. Sect. D, 69, 901-913.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.4.23.4 food industry the enzyme is used industrially in cheese production Bos taurus
3.4.23.4 food industry the enzyme is used industrially in cheese production Camelus dromedarius

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.4 doubly and singly glycosylated variants of chymosin, vapor diffusion method, using 2 M ammonium sulfate, 100 mM bis-Tris buffer in the pH range 5.1-6.5 Camelus dromedarius
3.4.23.4 unglycosylated chymosin, vapor diffusion method, using 100 mM NaH2PO4 pH 5.5, 1.5 M NaCl Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.23.4 additional information the loss of the first three residues of camel chymosin significantly decreases enzyme activity Camelus dromedarius

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.23.4 kappa-casein + H2O Bos taurus the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus ?
-
 ?
3.4.23.4 kappa-casein + H2O Camelus dromedarius the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.4 Bos taurus P00794
-
-
3.4.23.4 Camelus dromedarius Q9GK11
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.4 glycoprotein glycosylation at Asn291 significantly decreases enzyme activity Bos taurus
3.4.23.4 glycoprotein glycosylation at Asn291 significantly decreases enzyme activity Camelus dromedarius

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.4 phenyl Superose column chromatography Bos taurus
3.4.23.4 phenyl Superose column chromatography Camelus dromedarius

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.4 kappa-casein + H2O the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus Bos taurus ?
-
 ?
3.4.23.4 kappa-casein + H2O the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus Camelus dromedarius ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.23.4 ? x * about 40000, mass spectrometry Bos taurus
3.4.23.4 ? x * about 40000, mass spectrometry Camelus dromedarius

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.23.4 60
-
 melting temperature of the singly glycosylated enzyme Camelus dromedarius