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Information on EC 3.4.23.4 - chymosin and Organism(s) Camelus dromedarius and UniProt Accession Q9GK11
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3.4.23.4 chymosinSpecify your search results
Word Map
- 3.4.23.4
- milk
- casein
-
cheese
- pepsin
-
calf
-
coagulation
- kappa-caseins
- rennet
-
milk-clotting
- clot
- proteinases
- angiotensin
- hypertension
- aldosterone
- beta-caseins
-
micelle
- whey
- pepsinogen
- renin
-
ripening
- plasmin
- zymogen
-
curd
- camel
-
skim
- mucor
-
cheddar
- pepstatin
- abomasum
-
gelation
- cardunculus
-
preruminant
-
cynara
- progastricsins
- miehei
-
fundic
-
beta-cn
- food industry
- pusillus
- gastricsins
-
urea-page
-
s1-casein
- beta-lactoglobulin
- parasitica
- hypokalemia
- glycomacropeptide
-
cheese-making
- rhizomucor
-
3.4.23.1
- synthesis
The taxonomic range for the selected organisms is: Camelus dromedarius
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single Ser-Phe105-/-Met-Ala bond in kappa-chain of casein
Synonyms
chymosin, prochymosin, rennin, chymosin a, chymosin b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chymase
-
-
-
-
Preprorennin
-
-
-
-
rennin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-98-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
the enzyme cleaves the Phe105-Met106 bond of kappa-casein
-
-
?
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein
?
-
synthetic substrate
-
-
?
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein + H2O
?
-
-
-
-
?
undecapeptide analogue to chymosin sensitive region of camel kappa-casein
?
-
synthetic substrate
-
-
?
undecapeptide analogue to chymosin sensitive region of camel kappa-casein + H2O
?
-
-
-
-
?
kappa-casein + H2O
?
the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
-
-
?
additional information
?
-
does not cleave alpha-casein and beta-casein
-
-
?
additional information
?
-
camel chymosin is also a good coagulant for bovine milk
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
the enzyme cleaves the Phe105-Met106 bond of kappa-casein
-
-
?
additional information
?
-
does not cleave alpha-casein and beta-casein
-
-
?
kappa-casein + H2O
?
the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
maximum milk clotting activity is detected with 20-40 mM Ca2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
when subjected to a low pH, recombinant prochymosin is converted into mature and active chymosin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.077
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein
-
-
-
0.056
undecapeptide analogue to chymosin sensitive region of camel kappa-casein
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.7
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein
-
-
-
5.1
undecapeptide analogue to chymosin sensitive region of camel kappa-casein
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1 - 6.7
at pH 5.1, the relative clotting activity decreases to 50% and further declines to 17% and 10% at pH 5.6 and pH 6.7, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein
47
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of camel kappa casein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 60
relative activity of 50% is observed at temperatures of 35°C and 60°C. Chymosin activity completely ceases below 20°C or above 70°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CHYM_CAMDR
381
0
42083
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
-
apparent molecular weight, determined by comparison to a Novex Mark12TM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
doubly glycosylated camel chymosin has slightly higher catalytic efficiency
glycoprotein
glycosylation at Asn291 significantly decreases enzyme activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the loss of the first three residues of camel chymosin significantly decreases enzyme activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 6.5
the recombinant enzyme is highly active and stable over a wide pH range (from 2.5 to 6.0) at 20°C for 8 h. Relative clotting activity declines when the recombinant chymosin is kept at a pH value above 6.0. No detectable clotting activity at pH 6.5
732866
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 50
after 8 h of incubation, between 0 and 20°C the enzyme shows 100% activity, while at 30°C and 40°C 70% and 35% is retained, respectively. The enzyme is inactive after 8 h at 50°C
40 - 55
-
no residual clotting activities at temperatures higher than 55°C
56
-
chymosin-mediated hydrolysis of alphas1 casein is slower in cheeses treated at 56°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
the enzyme is used industrially in cheese production
food industry
additional information
-
under typical cheese-making conditions (pH 6.6, 0-2 mM CaCl2) the clotting activity of camel chymosin is ca. 80% higher than the activity of bovine chymosin (average clotting activity of camel chymosin is 70% higher than the activity of bovine chymosin), camel chymosin is more thermostable than bovine chymosin
food industry
-
chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making
food industry
-
the enzyme is used for the production of Reggianito cooked cheese
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kappeler, S.R.; van den Brink, H.J.; Rahbek-Nielsen, H.; Farah, Z.; Puhan, Z.; Hansen, E.B.; Johansen, E.
Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk
Biochem. Biophys. Res. Commun.
342
647-654
2006
Bos taurus, Camelus dromedarius
Sorensen, J.; Palmer, D.S.; Qvist, K.B.; Schiott, B.
Initial stage of cheese production: a molecular modeling study of bovine and camel chymosin complexed with peptides from the chymosin-sensitive region of kappa-casein
J. Agric. Food Chem.
59
5636-5647
2011
Bos taurus (P00794), Bos taurus, Camelus dromedarius (Q9GK11)
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
Acta Crystallogr. Sect. D
69
901-913
2013
Bos taurus (P00794), Bos taurus, Camelus dromedarius (Q9GK11)
Moller, K.K.; Rattray, F.P.; Sorensen, J.C.; Ardoe, Y.
Comparison of the hydrolysis of bovine kappa-casein by camel and bovine chymosin: a kinetic and specificity study
J. Agric. Food Chem.
60
5454-5460
2012
Bos taurus, Camelus dromedarius
Costabel, L.M.; Bergamini, C.V.; Pozza, L.; Cuffia, F.; Candioti, M.C.; Hynes, E.
Influence of chymosin type and curd scalding temperature on proteolysis of hard cooked cheeses
J. Dairy Res.
82
375-384
2015
Camelus dromedarius
Jensen, J.L.; Jacobsen, J.; Moss, M.L.; Rasmussen, F.; Qvist, K.B.; Larsen, S.; van den Brink, J.M.
The function of the milk-clotting enzymes bovine and camel chymosin studied by a fluorescence resonance energy transfer assay
J. Dairy Sci.
98
2853-2860
2015
Bos taurus, Camelus dromedarius
Wang, N.; Wang, K.Y.; Li, G.; Guo, W.; Liu, D.
Expression and characterization of camel chymosin in Pichia pastoris
Protein Expr. Purif.
111
75-81
2015
Camelus dromedarius (Q9GK11)
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