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Information on EC 3.4.23.4 - chymosin
for references in articles please use BRENDA:EC3.4.23.4
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.23 Aspartic endopeptidases
3.4.23.4 chymosin
IUBMB Comments
Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin. Found among mammals with postnatal uptake of immunoglobulins. In peptidase family A1(pepsin A family)
The enzyme appears in viruses and cellular organisms
- 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
Reaction Schemes
showBroad 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
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
calf chymosin
Chn
chymase
-
-
-
-
chymosin A
chymosin B
CYM
EC 3.4.4.3
-
-
formerly
-
Preprorennin
-
-
-
-
prochymosin
rCH
rennin
additional information
acid protease, major component of rennet (milk clotting enzyme)
prochymosin
-
cDNA predicted to code for 365 amino acids with a 42 amino acids long pro-region
rennin
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
endopeptidase
-
hydrolysis of peptide bond
-
-
peptides, endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-98-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
Substrates: low molecular weight, fluorogenic peptide substrate
Products: -
Products: -
?
Abz-A-A-F-F-A-A-p-nitroanilide + H2O
?
-
Substrates: low molecular weight, fluorogenic peptide substrate
Products: -
Products: -
?
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
Substrates: low molecular weight, fluorogenic peptide substrate
Products: -
Products: -
?
Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
Substrates: low molecular weight, fluorogenic peptide substrate
Products: -
Products: -
?
Abz-A-A-F-F-pnA + H2O
?
-
Substrates: low molecular weight, fluorogenic peptide substrate
Products: -
Products: -
?
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
Substrates: low molecular weight, fluorogenic peptide substrate
Products: -
Products: -
?
AFPLEFEREL + H2O
AFPLEF + EREL
Substrates: modified peptide substrate based on residues 165-174 of proopiomelanocortin
Products: -
Products: -
?
AFPLEFFREL + H2O
AFPLEF + FREL
Substrates: modified peptide substrate based on residues 165-174 of proopiomelanocortin
Products: -
Products: -
?
AFPLEFIREL + H2O
AFPLEF + IREL
Substrates: modified peptide substrate based on residues 165-174 of proopiomelanocortin
Products: -
Products: -
?
AFPLEFKREL + H2O
AFPLEF + KREL
Substrates: modified peptide substrate based on residues 165-174 of proopiomelanocortin
Products: -
Products: -
?
basic FGF 110-118 + H2O
?
-
Substrates: parent peptide and Leu115 and Lys115 variants respectively as substrate
Products: -
Products: -
?
beta-chain of proteolytic insulin + H2O
?
-
Substrates: general proteolytic activity
Products: -
Products: -
?
bovine kappa-casein residues 97-112 + H2O
?
-
Substrates: substrate binds in an extended conformation with charged residues on either side of the scissile bond playing an important role in stabilizing the binding pose. Substrate residues Lys111 and Lys112 bind to the N-terminal domain of chymosin displacing a conserved water molecule. A cluster of histidine and proline residues, His98-Pro99-His100-Pro101-His102, in kappa-casein binds to the C-terminal domain of the protein, where neighboring conserved arginine residue Arg97 is important for stabilizing the binding pose. The catalytic site including the catalytic water molecule is stable in the starting conformation of the general acid/base catalytic mechanism for 18 ns of molecular dynamics simulations
Products: -
Products: -
?
Dabcyl-HPHPHLSFMAIPK (5-FAM) KK-NH2 + H2O
?
Substrates: Dabcyl = 4-(dimethylaminoazo) benzene-4-carboxylic acid, 5-FAM = 5-carboxyfluorescein, fluorogenic substrate, reaction assay at pH 5.6, 25°C
Products: -
Products: -
?
dynorphin A 1-7e + H2O
?
-
Substrates: Ala3Phe7 and ILe3Lys5Phe7 variants respectively as substrate
Products: -
Products: -
?
His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
His-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
Substrates: part of the bovine kappa-casein sequence
Products: -
Products: -
?
His-Pro-His-Pro-His-Leu-Ser-Phe-Phe(NO2)-Ala-Ile-Pro-Pro-Lys-Lys + H2O
?
-
Substrates: -
Products: -
Products: -
?
kappa-casein + H2O
para-kappa-casein + glycopeptide
Substrates: cleavage between Phe105-Met106
Products: -
Products: -
?
kappa-casein + H2O
para-kappa-casein + macropeptide
-
Substrates: kappa-casein is the primary substrate for the chymosin action
Products: -
Products: -
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-S-F-M-A-I-P-NH2 + H2O
?
-
Substrates: hepapeptide, a fragment of the native chymosin substrate kappa-casein, is most efficiently cleaved by native calf chymosin and less efficiently by transgenic chymosin and recombinant chymosin
Products: -
Products: -
?
Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
-
Substrates: part of the bovine kappa-casein sequence
Products: -
Products: -
?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
Substrates: part of the bovine kappa-casein sequence
Products: -
Products: -
?
Leu-Ser-Phe-Met-Ala-O-methyl ester + H2O
Leu-Ser-Phe + Met-Ala-O-methyl ester
-
Substrates: part of the bovine kappa-casein sequence
Products: -
Products: -
?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
-
Substrates: -
Products: -
Products: -
?
Lys-Pro-Leu-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Leu-Glu-Phe + Phe(NO2)-Arg-Leu
-
Substrates: -
Products: -
Products: -
?
NT/NMN 142-151 + H2O
?
-
Substrates: parent peptide, Glu148 and Phe148 variants respectively as substrate
Products: -
Products: -
?
o-aminobenzoyl-Ala-Ala-Phe-Phe-Ala-Ala-NH-C6H4NO2 + H2O
o-aminobenzoyl-Ala-Ala-Phe + Phe-Ala-Ala-NHC6H4NO2
-
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-Ala-Ala-Phe-Phe-NH-C6H4-NO2 + H2O
o-aminobenzoyl-Ala-Ala-Phe + Phe-NH-C6H4-NO2
-
Substrates: -
Products: -
Products: -
?
POm C165-174 + H2O
?
-
Substrates: parent peptide and Glu171 variant respectively as substrate
Products: -
Products: -
?
Pro-His-Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Pro-His-Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
-
Substrates: part of the bovine kappa-casein sequence
Products: -
Products: -
?
Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Ser-Phe + Met-Ala-Ile-O-methyl ester
-
Substrates: part of the bovine kappa-casein sequence
Products: -
Products: -
?
Substance P + H2O
?
-
Substrates: parent peptide and Lys8 variant respectively as substrate
Products: -
Products: -
?
undecapeptide analogue to chymosin sensitive region of bovine kappa casein
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein + H2O
?
-
Substrates: -
Products: -
Products: -
?
undecapeptide analogue to chymosin sensitive region of camel kappa casein
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
undecapeptide analogue to chymosin sensitive region of camel kappa-casein
?
-
Substrates: synthetic substrate
Products: -
Products: -
?
undecapeptide analogue to chymosin sensitive region of camel kappa-casein + H2O
?
-
Substrates: -
Products: -
Products: -
?
YGISSKFCE + H2O
YGISSKF + L-Cys-L-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFfE + H2O
YGISSKF + FE
-
Substrates: modified peptide based on prochymosin sequence
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFHE + H2O
YGISSKF + His-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 51% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 51% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFIE + H2O
YGISSKF + Ile-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 54% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 54% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFKE + H2O
YGISSKF + Lys-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFLE + H2O
YGISSKF + L-Leu-L-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 42% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 42% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFME + H2O
YGISSKF + L-Met-L-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 52% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 52% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFNE + H2O
YGISSKF + L-Asn-L-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFRE + H2O
YGISSKF + Arg-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 59% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 59% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFVE + H2O
YGISSKF + Val-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 36% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 36% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFWE + H2O
YGISSKF + Trp-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
YGISSKFYE + H2O
YGISSKF + L-Tyr-L-Glu
-
Substrates: modified peptide based on prochymosin sequence
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
Products: 100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
?
alpha-casein + H2O
?
-
Substrates: at 50% casein degradation, 15% more of alphaS1-casein with eight phosphate groups is hydrolysed compared with alphaS1-casein with nine phosphate groups in chymosin-induced milk gels
Products: -
Products: -
?
alpha-casein + H2O
?
-
Substrates: alpha-casein is hydrolyzed extensively
Products: -
Products: -
?
alpha-casein + H2O
?
-
Substrates: alpha-casein is hydrolyzed extensively
Products: -
Products: -
?
beta-casein + H2O
?
-
Substrates: occurs during the long period of renneting
Products: -
Products: -
?
beta-casein + H2O
?
-
Substrates: in sodium caseinate solutions, more than 10% more beta-casein A2 is degraded compared with beta-casein A1 and B at 50% casein degradation
Products: -
Products: -
?
bovine kappa-casein + H2O
?
-
Substrates: kappa-casein samples are a mixture of monomers and aggregates at room temperature and pH 7.2, and that heating produces extensive kappa-casein aggregation.The initial polymerization or association state of kappa-casein affects on the aggregation stage after the enzymatic action of chymosin. Sucrose and lactose also affect the aggregation of proteolized particles of kappa-chymosin
Products: -
Products: -
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein
Products: -
Products: -
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein
Products: -
Products: -
?
casein + H2O
?
-
Substrates: the enzyme breaks the bond between Phe-105 and Met-106 in the casein and initiates the coagulation of milk
Products: -
Products: -
?
fluorescein thiocarbamoyl-kappa-casein + H2O
?
Substrates: -
Products: -
Products: -
?
fluorescein thiocarbamoyl-kappa-casein + H2O
?
Substrates: -
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
36869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36893, 36894
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: the enzyme cleaves the Phe105-Met106 bond
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: the bond Phe105-Met106 is the main hydrolyzed bond by the enzyme
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: the enzyme rapidly and specifically hydrolyzes kappa-CN's Phe105-Met106 bond, resulting in instability of casein micelles
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: the enzyme cleaves the Phe105-Met106 bond
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: chymosin hydrolyzes the F105-M106 bond in the kappa-casein molecule selectively and at a high rate, which causes milk clotting
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: 10% solution of standardized skimmed milk powder in 5 mM CaCl2, pH 6.5, is used as a substrate
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
casein macropeptide + para-kappa-casein
-
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
casein macropeptide + para-kappa-casein
-
Substrates: -
Products: -
Products: -
?
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
-
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
-
Substrates: -
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
Products: p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
Products: p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
milk + H2O
?
-
Substrates: the maximum increase on milk-clotting activity is 10% for recombinant chymosin at 212MPa/5 min/10°C
Products: -
Products: -
?
additional information
?
-
Substrates: in acidic conditions, the inactive proenzyme converts to the active form by autocatalytically cleavage of prosequence
Products: -
Products: -
?
additional information
?
-
-
Substrates: in acidic conditions, the inactive proenzyme converts to the active form by autocatalytically cleavage of prosequence
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has milk coagulation bioactivity
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the process of milk coagulation under the action of chymosin, alpha- and beta-caseins are not hydrolyzed
Products: -
Products: -
?
additional information
?
-
Substrates: bovine chymosin is a poor coagulant for camel milk
Products: -
Products: -
?
additional information
?
-
-
Substrates: bovine chymosin is a poor coagulant for camel milk
Products: -
Products: -
?
additional information
?
-
Substrates: influence of chymosin on physicochemical and hydrolysis characteristics of casein (CN) micelles in skim milk and individual caseins, overview. Chymosin hydrolyzes individual beta-casein, kappa-casein, and alpha-S-casein, but not beta-lactoglobulin. The hydrolysis of kappa-CN by chymosin occurs before that of beta-CN and alpha-S-CN. beta-CN and alpha-S-CN are connected with colloidal calcium phosphate
Products: -
Products: -
-
additional information
?
-
Substrates: does not cleave alpha-casein and beta-casein
Products: -
Products: -
?
additional information
?
-
Substrates: camel chymosin is also a good coagulant for bovine milk
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant roe deer and cow Chns have similar proteolytic specificity and are able to hydrolyze not only kappa-CN but also alpha- and beta-caseins during the assay time
Products: -
Products: -
-
additional information
?
-
-
Substrates: the ROCC clotting activity on donkey, cow, goat, lamb, camel milk is determined as 40, 10, 5.7, 3.07, and 2.66 IMCU/ml, respectively
Products: -
Products: -
-
additional information
?
-
-
Substrates: in the process of milk coagulation under the action of chymosin, alpha- and beta-caseins are not hydrolyzed
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
kappa-casein + H2O
casein macropeptide + para-kappa-casein
-
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
-
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
para-kappa-casein + glycopeptide
Substrates: cleavage between Phe105-Met106
Products: -
Products: -
?
milk + H2O
?
-
Substrates: the maximum increase on milk-clotting activity is 10% for recombinant chymosin at 212MPa/5 min/10°C
Products: -
Products: -
?
alpha-casein + H2O
?
-
Substrates: alpha-casein is hydrolyzed extensively
Products: -
Products: -
?
alpha-casein + H2O
?
-
Substrates: alpha-casein is hydrolyzed extensively
Products: -
Products: -
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein
Products: -
Products: -
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein
Products: -
Products: -
?
casein + H2O
?
-
Substrates: the enzyme breaks the bond between Phe-105 and Met-106 in the casein and initiates the coagulation of milk
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
36869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36893, 36894
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: the enzyme cleaves the Phe105-Met106 bond
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: the enzyme cleaves the Phe105-Met106 bond
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
Substrates: cleaves a single bond between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: chymosin hydrolyzes the F105-M106 bond in the kappa-casein molecule selectively and at a high rate, which causes milk clotting
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
kappa-casein + H2O
?
-
Substrates: cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has milk coagulation bioactivity
Products: -
Products: -
?
additional information
?
-
Substrates: does not cleave alpha-casein and beta-casein
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
-
Cu2+, Mn2+, and Co2+ ions have no effect on the enzyme activity
Ca2+
maximum milk clotting activity is detected with 20-40 mM Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Blood serum
-
porcine and particularly equine serum impairs the coagulation of milk by chymosin, the inhibitor(s) may be heat labile, alpha2-macroglobulin may be the inhibitory substance
-
EDTA
-
10 mM EDTA causes inhibition of 73.8% of the milk-clotting activity
iodoacetamide
-
4 mM iodoacetamide causes inhibition of 7.2% of the milk-clotting activity
Ni2+
introduction of Ni2+ into milk inhibits the coagulation ability of moose chymosin
additional information
-
phenylmethylsulfonyl fluoride does not affect the enzyme activity
-
Ca2+
-
milkclotting activity decrease when the concentration of Ca2+ is higher than 40 mM
Ca2+
-
Ca2+ inhibits milk-clotting activity (about 50% residual activity at 5 mM)
pepstatin
-
inhibits recombinant and transgenic chymosin less efficiently than the native enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
activates, dependence of milk-clotting activity on the concentration of calcium chloride. Ca2+ partially shields the negative charge of the C-terminal regions of kappa-casein, which form a hair layer on the surface of casein micelles. As a result, the Phe105-Met106 bond becomes more accessible to attack from the milk-clotting enzyme. Second, Ca2+ is involved in the formation of ionic bridges between destabilized micelles, which accelerates their aggregation and the formation of a milk clot. The addition of CaCl2 is widely used in the cheese making to improve the technological properties of rennet-lean milk
kappa-casein
a HPHPH sequence in the P8-P4 residues of the natural substrate kappa-casein acts as the allosteric activator of the enzyme
-
additional information
introduction of Mg2+, Zn2+, Co2+, Ba2+, Fe2+, Mn2+, Ca2+, and Cu2+ into milk activates the coagulation ability of moose chymosin
-
additional information
when subjected to a low pH, recombinant prochymosin is converted into mature and active chymosin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Immunocytochemical evidence for gastric proteases in adenocarcinoma of the stomach.
Alkalosis
The importance of genetic counseling and genetic screening: a case report of a 16-year-old boy with resistant hypertension and severe hypokalemia.
Alkalosis
[A case of severe hypokalemia caused by a Chinese herbal remedy (Yokukansan) in an 81-year-old woman with dementia].
Alkalosis
[Renovascular hypertension due to unilateral renal artery stenosis with hypokalemic alkalosis, the salt-losing syndrome and reversible hyperechogenicity of the contralateral kidney. A study of 2 infants]
Anemia, Pernicious
The Glands of the Stomach in Relation to Pernicious Anaemia; with Special Reference to the Glands in the Pyloric Region: (Section of Medicine).
Cardiovascular Diseases
Valsartan chronotherapy reverts the non-dipper pattern and improves blood pressure control through mediation of circadian rhythms of the renin-angiotensin system in spontaneous hypertension rats.
Cysts
THE NEOPLASTIC POTENTIALITIES OF MOUSE EMBRYO TISSUES : III. THE TUMORS ELICITED FROM GASTRIC EPITHELIUM.
Enteritis
Contribution to some phenotypical characteristics of Vibrio cincinnatiensis. Studies in one strain of a diarrhoeic human patient and in two isolates from aborted bovine fetuses.
Genetic Diseases, Inborn
[Liddle syndrome as a rare cause of hypertension - a case report].
Hyperaldosteronism
A Rare Aldosterone-Producing Adenoma Detected by 68Ga-pentixafor PET-CT: A Case Report and Literature Review.
Hyperaldosteronism
Case Report: A case report of acromegaly associated with primary aldosteronism.
Hyperaldosteronism
[A case of severe hypokalemia during emergency surgery caused by long-term administration of Shakuyaku-kanzo-to].
Hyperaldosteronism
[A rare case of primary aldosteronism caused by bilateral functioning adrenocortical adenomas with renal cell carcinoma]
Hyperaldosteronism
[Evaluation of the ratio of plasma aldosterone to rennin concentration measured by an automated chemiluminescent immunoassay in screening for primary aldosteronism].
Hyperaldosteronism
[The accuracy of combining aldosterone to renin ratio and low renin level in diagnosing primary aldosteronism]
Hypertension
A case of primary aldosteronism caused by multiple adrenocortical macronodules.
Hypertension
A systematic review on randomized control trials on rennin angiotensin aldosterone system inhibitors role in managing hypertension among hemodialysis patients.
Hypertension
Hypotensive effects of renal denervation in spontaneously hypertensive rat based on ultrasonic contrast imaging.
Hypertension
Recanalization and stenting of total occlusions of the renal arteries for blood pressure control in resistant to treatment hypertension.
Hypertension
The importance of genetic counseling and genetic screening: a case report of a 16-year-old boy with resistant hypertension and severe hypokalemia.
Hypertension
Valsartan chronotherapy reverts the non-dipper pattern and improves blood pressure control through mediation of circadian rhythms of the renin-angiotensin system in spontaneous hypertension rats.
Hypertension
[Adenosine receptors agonists mitigated PAH of rats induced by chronic hypoxia through reduction of renin activity/angiotensin II levels and increase of inducible nitric oxide synthase-nitric oxide levels].
Hypertension
[Renovascular hypertension due to unilateral renal artery stenosis with hypokalemic alkalosis, the salt-losing syndrome and reversible hyperechogenicity of the contralateral kidney. A study of 2 infants]
Hypertension
[Retroperitoneal laparoscopic management of primary aldosteronism with report of 130 cases]
Hypertension
[Subclinical endothelial inflammation markers in a family with type I familial hyperaldosteronism caused by a de novo mutation]
Hypertension, Pulmonary
[Effects of continuous adenosine infusion on pulmonary hypertension in chronically hypoxic rats]
Hypertrophy, Left Ventricular
[Heat shock proteins 70 kD as a new marker of lesions to target organs in hypertension]
Hypoaldosteronism
[A case of severe hypokalemia caused by a Chinese herbal remedy (Yokukansan) in an 81-year-old woman with dementia].
Hypokalemia
A case of primary aldosteronism caused by multiple adrenocortical macronodules.
Hypokalemia
The importance of genetic counseling and genetic screening: a case report of a 16-year-old boy with resistant hypertension and severe hypokalemia.
Hypokalemia
[A case of severe hypokalemia caused by a Chinese herbal remedy (Yokukansan) in an 81-year-old woman with dementia].
Hypokalemia
[Fifty years of subclinical primary aldosteronism: importance of early diagnosis].
Hypokalemia
[Retroperitoneal laparoscopic management of primary aldosteronism with report of 130 cases]
Hyponatremia
[Renovascular hypertension due to unilateral renal artery stenosis with hypokalemic alkalosis, the salt-losing syndrome and reversible hyperechogenicity of the contralateral kidney. A study of 2 infants]
Hypothyroidism
Arterial hypertension and thyroid disorders: What is important to know in clinical practice?
Insulin Resistance
[Effect of modified liberation doxazosin on blood pressure, insulin resistance, and catecholamine secretion in patients with true resistant hypertension]
Ischemic Stroke
[The balance of markers of regulation vascular tone and fibrinogen in the prognosis of hemorrhagic transformation and fatal outcome in the acute period of ischemic stroke].
Lipid Metabolism Disorders
Function of Uric Acid Transporters and Their Inhibitors in Hyperuricaemia.
Liver Diseases
Study of substance P, renin and aldosterone in chronic liver disease in Egyptian children.
Liver Neoplasms
Novel Bacillus Milk-Clotting Enzyme Produces Diverse Functional Peptides in Semihard Cheese.
Measles
Avoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies?
Mumps
Avoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies?
Neoplasms
Immunocytochemical evidence for gastric proteases in adenocarcinoma of the stomach.
Neoplasms
[A case of ruptured multiple cerebral aneurysms associated with primary aldosteronism]
Peritoneal Fibrosis
MicroRNA-21 contributes to high glucose-induced fibrosis in peritoneal mesothelial cells in rat models by activation of the Ras-MAPK signaling pathway via Sprouty-1.
Polyuria
[Renovascular hypertension due to unilateral renal artery stenosis with hypokalemic alkalosis, the salt-losing syndrome and reversible hyperechogenicity of the contralateral kidney. A study of 2 infants]
Pre-Eclampsia
The relationship between aldosterone to renin ratio and RI value of the uterine artery in the preeclamptic patient vs. normal pregnancy.
Pulmonary Fibrosis
Recent reports about enzymes related to the synthesis of prostaglandin (PG) F(2) (PGF(2?) and 9?, 11?-PGF(2)).
Renal Artery Obstruction
[Renovascular hypertension due to unilateral renal artery stenosis with hypokalemic alkalosis, the salt-losing syndrome and reversible hyperechogenicity of the contralateral kidney. A study of 2 infants]
Renal Insufficiency, Chronic
Valsartan chronotherapy reverts the non-dipper pattern and improves blood pressure control through mediation of circadian rhythms of the renin-angiotensin system in spontaneous hypertension rats.
Rubella
Avoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies?
Sexually Transmitted Diseases
Avoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies?
Sleep Apnea, Obstructive
[The changes of some vasoactive substances after operation in patients with obstructive sleep apnea-hypopnea syndrome]
Sleep Deprivation
Effects of mental resilience on neuroendocrine hormones level changes induced by sleep deprivation in servicemen.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
0.165
undecapeptide analogue to chymosin sensitive region of bovine kappa casein
-
-
-
0.077
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein
-
-
-
0.134
undecapeptide analogue to chymosin sensitive region of camel kappa casein
-
-
-
0.056
undecapeptide analogue to chymosin sensitive region of camel kappa-casein
-
-
-
0.0056
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by transgenic chymosin
0.0056
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by recombinant chymosin
0.007
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
0.0022
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
0.0035
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by recombinant chymosin
0.018
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by transgenic chymosin
0.0018
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
0.0021
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by recombinant chymosin
0.0078
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by transgenic chymosin
0.016
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by D289M/Q298L mutant chymosin
0.024
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by D289M/Q298L mutant chymosin
0.028
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by Asp289Met mutant chymosin
0.029
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by Gln298Leu mutant chymosin
0.033
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by Gln298Leu mutant chymosin
0.046
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by D289M/Q298L mutant chymosin
0.054
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by Asp289Met mutant chymosin
0.054
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by Asp289Met mutant chymosin
0.059
NT/NMN 142-151
-
hydrolysis of the parent peptide by wild type chymosin
0.062
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by Gln298Leu mutant chymosin
0.072
NT/NMN 142-151
-
hydrolysis of the parent peptide by Asp289Met mutant chymosin
0.083
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by wild type chymosin
0.087
NT/NMN 142-151
-
hydrolysis of the parent peptide by D289M/Q298L mutant chymosin
0.095
NT/NMN 142-151
-
hydrolysis of the parent peptide by Gln298Leu mutant chymosin
0.105
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by wild type chymosin
0.111
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by wild type chymosin
0.065
POm C165-174
-
hydrolysis of the Glu171 variant by Asp289Met mutant chymosin
0.114
POm C165-174
-
hydrolysis of the Glu171 variant by D289M/Q298L mutant chymosin
0.229
POm C165-174
-
hydrolysis of the parent peptide by Gln298Leu mutant chymosin
0.25
POm C165-174
-
hydrolysis of the parent peptide by D289M/Q298L mutant chymosin
0.288
POm C165-174
-
hydrolysis of the parent peptide by Asp289Met mutant chymosin
0.304
POm C165-174
-
hydrolysis of the Glu171 variant by wild type chymosin
0.375
POm C165-174
-
hydrolysis of the parent peptide by wild type chymosin
0.463
POm C165-174
-
hydrolysis of the Glu171 variant by Gln298Leu mutant chymosin
additional information
additional information
-
Km of kappa-casein related peptides
-
additional information
additional information
-
transgenic and recombinant chymosin do not hydrolyze substrate Abz-A-A-F-F-A-A-p-nitroanilide, Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine and Abz-A-A-F-F-p-nitroanilide
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
44.3
undecapeptide analogue to chymosin sensitive region of bovine kappa casein
-
-
-
11.7
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein
-
-
-
4.3
undecapeptide analogue to chymosin sensitive region of camel kappa casein
-
-
-
5.1
undecapeptide analogue to chymosin sensitive region of camel kappa-casein
-
-
-
0.12
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by recombinant chymosin
0.16
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by transgenic chymosin
1.6
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
0.02
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by transgenic chymosin
0.11
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by recombinant chymosin
0.8
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
0.06
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by transgenic chymosin or recombinat chymosin
0.14
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine
-
hydrolysis by calf chymosin
2 - 8
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by wild type chymosin
12
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by Gln298Leu mutant chymosin
16
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by D289M/Q298L mutant chymosin
17
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by Gln298Leu mutant chymosin
17
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by D289M/Q298L mutant chymosin
22
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by D289M/Q298L mutant chymosin
27
NT/NMN 142-151
-
hydrolysis of the parent peptide by D289M/Q298L mutant chymosin
30
NT/NMN 142-151
-
hydrolysis of the parent peptide by Gln298Leu mutant chymosin
32
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by Asp289Met mutant chymosin
35
NT/NMN 142-151
-
hydrolysis of the parent peptide by Asp289Met mutant chymosin
39
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage L147-F148) by Asp289Met mutant chymosin
41
NT/NMN 142-151
-
hydrolysis of the parent peptide by wild type chymosin
42
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by Asp289Met mutant chymosin
46
NT/NMN 142-151
-
hydrolysis of the Glu148 variant by wild type chymosin
49
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by Gln298Leu mutant chymosin
191
NT/NMN 142-151
-
hydrolysis of the Phe148 variant (cleavage F147-R148) by wild type chymosin
12
POm C165-174
-
hydrolysis of the Glu171 variant by D289M/Q298L mutant chymosin
14
POm C165-174
-
hydrolysis of the Glu171 variant by Asp289Met mutant chymosin
43
POm C165-174
-
hydrolysis of the parent peptide by D289M/Q298L mutant chymosin
52
POm C165-174
-
hydrolysis of the Glu171 variant by Gln298Leu mutant chymosin
90
POm C165-174
-
hydrolysis of the parent peptide by Gln298Leu mutant chymosin
101
POm C165-174
-
hydrolysis of the parent peptide by Asp289Met mutant chymosin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.272
-
after 33.2fold purification, in 50 mM acetate buffer (pH 5.6) at 37°C
additional information
additional information
the crude recombinant chymosin has a milk-clotting activity of 86 AU/ml, purified genetically engineered moose chymosin has a specific milk-clotting activity of 15768 AU/mg
additional information
crude extracts of camel chymosin show 50 IMUC/l milk
additional information
-
total milk-clotting activity of recombinant roe deer chymosin is estimated to be 468.4 IMCU/ml
additional information
total milk-coagulation activity (MCA) of the recombinant maral chymosin is 2330 AU/ml. The recombinant maral prochymosin relative activity is 52955 AU/mg
additional information
-
the ROCC clotting activity on donkey, cow, goat, lamb, camel milk is determined as 40, 10, 5.7, 3.07, and 2.66 IMCU/ml, respectively
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
-
for proteolysis of undecapeptide analogue to chymosin sensitive region of the bovine kappa casein
5.1
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein
5.5
5.65
6 - 7
6.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 5
-
acid-denatured hemoglobin, pH 1: about 80% of maximum activity, pH 5: about 30% of maximum activity
2 - 6.7
4 - 8
the enzyme shows about 60% activity at pH 4.0, about 80% activity at pH 5.5, 100% activity at pH 6.0, about 95% activity at pH 7.0, about 38% activity at pH 7.5, and about 20% activity at pH 8.0
5 - 6.5
the enzyme retains about 65%, 100%, 85% and 69% of milk clotting activity at pH 5.0, 5.5, 6.0 and 6.5, respectively
5 - 9
-
the Tol-A-III-chymosin fusion protein shows more than 60% activity between pH 5.0 and 9.0
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
5.5
5.5 - 6
5.5 - 8
sharp decline of activity up to pH 5.8, moderate decline at higher pH with complete loss of activity at pH 8
5.5 - 6
-
100% activity at pH 5.5, about 90% activity at pH 6.0, about 30% activity at pH 6.5, the enzyme almost completely loses its activity at pH 7.0
5.5 - 6
-
100% activity at pH 5.5, about 20% activity at pH 6.0, the enzyme almost completely loses its activity at pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
42
47
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of camel kappa casein
56
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of camel kappa casein
additional information
42
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein
42
-
for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein
additional information
the substrate temperature was found to influence milk clotting activity, optimum substrate temperature is 65°C
additional information
-
the substrate temperature was found to influence milk clotting activity, optimum substrate temperature is 65°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
the enzyme shows more than 90% activity over a temperature range of 30-45°C and about 75% activity at 20°C and 50°C
20 - 60
25 - 65
-
activity range, profile overview. High activity at 35-45°C, 25% activity at 50°C
30 - 50
maximal activity at 30°C, 81% of maximal activity at 50°C, complete inactivation at 70°C
30 - 55
-
the Tol-A-III-chymosin fusion protein shows high activity between 30 and 55°C
30 - 60
milk clotting activity declines moderately up to 55°C (80% of maximum activity) and than drops to 40% of activity at 60°C proteolytic activity at 30°C and 60°C approximately 80% of maximum activity
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
additional information
20 - 60
the enzyme shows about 30% activity at 20°C, about 85% activity at 30°C, 100% activity at 40°C, about 70% activity at 50°C and about 60% activity at 60°C
additional information
the substrate temperature was found to influence milk clotting activity, sharp optimum at 65°C with complete loss of activity at 75°C, less than 20% of activity at 30°C
additional information
-
the substrate temperature was found to influence milk clotting activity, sharp optimum at 65°C with complete loss of activity at 75°C, less than 20% of activity at 30°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
35015, 36869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36891, 36892, 36893, 36894, 667435, 667763, 668957, 669642, 687952, 707523, 708213, 708236
-
-
brenda
chymosin derived as commercial enzyme preparation (Maxiren) from a genetically modified yeast Kluyveromyces lactic
-
-
brenda
use of a synthetic gene that encodes a protein identical to bovine prochymosin
-
-
brenda
synthetic construct of prochymosin mRNA; enzyme secretion is maximal during the first days after birth, enzyme level declines thereafter and chymosin in replaced by pepsin
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the enzyme is secreted in the fourth stomach of newborn ruminants
brenda
produced in the fourth stomach of milk fed ruminants as inactive precursor prochymosin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
rennet from abomasal tissue from a local indigenous breed
-
brenda
the enzyme is secreted into the calf's stomach
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
-
rabbit chymosin is more specific compared to bovine and camel chymosins when it comes to hydrolyzing alpha-, beta-, and kappa-casein
evolution
comparison of chymosin sequences and milk clotting kinetics from cow, camel and maral, overview
physiological function
-
chymosin, an aspartic protease, is the main enzymatic component of calf rennet
physiological function
-
one of the primary physiologic functions of Chn is its ability to coagulate milk in the stomach of newborns. As a result, proteins and other milk nutrients are retained longer in gastrointestinal tract, which ensures their complete digestion. Specific or milk coagulation activity is aimed at hydrolyzing only one (key) bond in the kappa-casein molecule. Proteolysis of this single bond destabilizes casein micelles, which allows them to converge forming a three-dimensional mesh-like structure, milk clot. In the case of bovine kappa-CN, the key bond is the F105-M106
physiological function
chymosin is the main enzyme responsible for milk protein coagulation. Chymosin is a protease found in rennet that can precipitate milk proteins and promote the formation of curds during cheese making Milk coagulation is a cycle in which liquid milk is turned into a viscoelastic semi-strong coagulum. Chymosin induces the hydrolysis of kappa-CN, which causes destabilization and aggregation of casein micelles. Proteolysis is considered to be the main biochemical pathway affecting the surface and flavor development during cheese making
additional information
effects of camel chymosin on physicochemical properties, e.g. the yield and hardness of camel and bovine cheeses, detailed overview. The high percentage of beta-casein might also contribute to the soft and smooth nature of camel cheeses, low kappa-casein content in camel milk compared to bovine milk. The camel milk cheeses are generally more acidic than bovine milk cheese
additional information
method development to analyse 15N/14N in chymosin after extraction, overview
additional information
camel chymosin is blended with calf chymosin for use in production of cheese from raw cow milk. Determination of the best mixture of coagulant for Beyaz peynir, in terms of proteolysis, texture, and melting characteristics, overview. Cheeses made with higher levels of calf chymosin produce higher levels of pH 4.6-SN and 12% TCASN fractions than cheeses made with camel chymosin. Cheeses containing a large amount of calf chymosin have higher levels of total FAA and higher meltability values than cheeses containing higher ratios of camel chymosin. The cheeses showing a high ratio of calf chymosin have higher residual coagulant activity. Cheeses produced by calf chymosin are harder than the camel chymosin counterparts. The same trend is observed for gumminess values, the cheeses containing calf chymosin at a high proportion have a softer structure compared with the cheeses containing a larger level of camel chymosin
additional information
camel chymosin is blended with calf chymosin for use in production of cheese from raw cow milk. Determination of the best mixture of coagulant for Beyaz peynir, in terms of proteolysis, texture, and melting characteristics, overview. Cheeses made with higher levels of calf chymosin produce higher levels of pH 4.6-SN and 12% TCASN fractions than cheeses made with camel chymosin. Cheeses containing a large amount of calf chymosin have higher levels of total FAA and higher meltability values than cheeses containing higher ratios of camel chymosin. The cheeses showing a high ratio of calf chymosin have higher residual coagulant activity. Cheeses produced by calf chymosin are harder than the camel chymosin counterparts. The same trend is observed for gumminess values, the cheeses containing calf chymosin at a high proportion have a softer structure compared with the cheeses containing a larger level of camel chymosin
additional information
particle size analysis of milk proteins and individual milk proteins treated with chymosin, overview
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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_BOVIN
381
0
42180
Swiss-Prot
Secretory Pathway (Reliability: 3)
A0A7D3Q7Y7_9CERV
381
0
42254
TrEMBL
Mitochondrion (Reliability: 4)
M4LK61_BOSMU
381
0
42208
TrEMBL
Secretory Pathway (Reliability: 1)
POL_HV1B1
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
1447
0
163288
Swiss-Prot
Secretory Pathway (Reliability: 3)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35600
36000
40000
42000
35600
-
when the proenzyme is brought to pH 4.2, removal of 42 N-terminal residues results in an active form of chymosin of 35600 Da
40000
-
apparent molecular weight, determined by comparison to a Novex Mark12TM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 48756, Tol-A-III-chymosin fusion protein, calculated from amino acid sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
glycoprotein
the preproenzyme has 2 glycosylation sites at N310Q and N349Q
glycoprotein
glycosylation at Asn291 significantly decreases enzyme activity
glycoprotein
-
doubly glycosylated camel chymosin has slightly higher catalytic efficiency
glycoprotein
glycosylation at Asn291 significantly decreases enzyme activity
proteolytic modification
zymogen activation takes place in an acidic environment involving cleavage of the N-terminal 42-residue propeptide that blocks the enzyme active site. As a result, prochymosin is transformed into the active enzyme, chymosin (Chn)
proteolytic modification
zymogen activation takes place in an acidic environment involving cleavage of the N-terminal 42-residue propeptide that blocks the enzyme active site. As a result, prochymosin is transformed into the active enzyme, chymosin (Chn)
additional information
-
insertion of a glycosylation site (S351T), glycosylation has significant inhibitory effect but this can be circumvented by deglycosylation with endoglucosidase H
additional information
bovine chymosin is a zymogen enzyme, consisting of pre- and pro-peptide segments before full maturation. The pre-peptide acts as a signal peptide, facilitating enzyme secretion into the calf's stomach. The pro-peptide, on the other hand, maintains the enzyme in an inactive state. When the enzyme is secreted into the calf's stomach, it spontaneously dissociates under acidic conditions, becoming active
additional information
-
zymogen prochymosin (rProChn) acidic activation leads to a 4600fold increased MCA, indicating high efficiency of conversion of the rProChn into the active roe deer rChn
additional information
-
activation of zymogen prochymosin is performed via acid treatment. In the acidification procedure, the pH of the supernatant is adjusted to pH 2.0 using 1 M HCl at 25°C with 2 h incubation time. In the neutralization procedure, the pH of the supernatant is raised to pH 5.5 using 1 M NaOH during 2 h
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of chymosin in complex with residues 97-112 of bovine kappa-casein. Substrate binds in an extended conformation with charged residues on either side of the scissile bond playing an important role in stabilizing the binding pose. Substrate residues Lys111 and Lys112 bind to the N-terminal domain of chymosin displacing a conserved water molecule. A cluster of histidine and proline residues, His98-Pro99-His100-Pro101-His102, in kappa-casein binds to the C-terminal domain of the protein, where neighboring conserved arginine residue Arg97 is important for stabilizing the binding pose. The catalytic site including the catalytic water molecule is stable in the starting conformation of the general acid/base catalytic mechanism for 18 ns of molecular dynamics simulations
-
unglycosylated chymosin, vapor diffusion method, using 100 mM NaH2PO4 pH 5.5, 1.5 M NaCl
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D304A/T218A
S351T
-
insertion of a glycosylation site in the linker region between chymosin and glucoamylase, strongly improves enzyme secretion
additional information
additional information
moose recombinant chymosin with a milk-clotting activity of 86 AU/ml is synthesized in the Kluyveromyces lactis expression system
additional information
-
Asp289Met mutant, Gln298Leu mutant, hydrolytic activity toward peptides having Lys at P'1 decreases significantly, mainly because of a decrease in the turnover values
additional information
the loss of the first three residues of camel chymosin significantly decreases enzyme activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 6
-
under incubation at 37°C for 24 and 48 h, loss of activity at pH 3.5 and pH 7.0, trangenic chymosin and recombinant chymosin are inactivated slightly faster than the native enzyme
2 - 6.5
-
crystalline chymosin exhibits optimum stability at pH between 5.3 and 6.3, the enzyme is moderately stable at pH 2.0, but the enzyme is unstable at pH around 3.5 and above 6.5, clotting activity is not observed at pH 7.0
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
3 - 6
-
recombinant enzyme, 37°C, 8h, stable, inactivation at pH 6.5-7.0
3.5 - 7
the enzyme remains stable (100% activity) for 1 h at pH 3.5-7.0. At pH 7.5 and 8.0, the activity drops to about 40% and 20%, respectively. The enzyme is inactive after 1 h at pH 9.0
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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
25
-
most stable at pH 5.0, denaturation can be fitted to the two-state irreversible model
25 - 50
-
transgenic chymosin loses activity slightly faster than abomasal enzyme and recombinant enzyme
35 - 55
-
the enzyme activity remains stable after 30 min at 35-55°C and drops to about 20% after 30 min at 60°C
4 - 70
after 1 h at 4, 10, 20, 30, 40, 50 and 60°C, the enzyme shows about 99%, 80%, 70%, 60%, 60%, 55% and 40% residual activity, respectively. The enzyme is inactive after 1 h at 70°C
40
-
the enzyme is stable until 40°C for 30 min while losing 40 and 80% of its activity after incubation at 45 and 50°C for 30 min, respectively
40 - 55
-
no residual clotting activities at temperatures higher than 55°C
50 - 60
-
chymosin is stable up to 50°C and a relative milk-clotting activity of 50% is recorded when the temperature is raised to 60°C
55
56
60
60 - 100
-
incubation at 60°C for 2 min 30 s decreases the mil clotting activity of the enzyme. A 2 min heating at 80 and 100°C totally inactivates the enzyme
75
-
it is not possible to coagulate milk with chymosin at 75°C due to its loss of activity
additional information
-
the enzyme undergoes irreversible, highly scan-rate-dependent thermal denaturation under all the experimental conditions investigated (pH 2-12, 20-50°C). Between pH 3.0 and 7.0, only one endotherm characterizes the thermal denaturation of the enzyme. Upon reaching pH 7.5, the denaturation is characterized by two endotherms
55
stable up to 55°C, more thermostable than cattle chymosin and equally stable as buffalo chymosin
56
-
chymosin-mediated hydrolysis of alphas1 casein is slower in cheeses treated at 56°C
56
-
chymosin-mediated hydrolysis of alphas1 casein is slower in cheeses treated at 56°C
60
the recombinant enzyme retains 42% of relative milk clotting activity at 60°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
for prochymosins activation, the supernatant is adjusted to pH 2.0 and incubated for 2 h at 25°C, then adjusted to pH 6.3 and left again at 25°C for 1 h
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
-
chymosin loses 50% of its activity after incubation in 4.6 M urea at 37°C for 30 min
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q Sepharose column chromatography, and Sephadex S-100 gel filtration
-
phenyl Superose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Pichia pastoris strain GS115
gene CYM, cloning and DNA and amino acid sequence determination and analyis, sequence comparisons, several polymorphisms were identified in the left fragment of the maral CYM gene: two regions of point deletions outside of the protein-coding regions and a pair of synonymous single nucleotide polymorphisms in exons. Gene alleles are separated by cloning of the CYM PCR product into the pJET vector and following sequencing of several DNA clones. Recombinant expression of maral prochymosin in Escherichia coli strain BL21(DE3)
gene CYM, codon optimization of native bovine prochymosin gene, recombinant enzyme expression in Nicotiana tabacum cv. Petit Havana via Agrobacterium tumefaciens strain LBA4404 transfection method, subcloning in Escherichia coli
gene CYM, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in CHO-K1 cells from pCMV(CAT)T7-SB100 plasmid, secretion of recombinant prochymosin into the culture fluid. Evaluation of the CHO-K1 expression system compared to other expression systems
-
gene CYM, recombinant enzyme expression in Kluyveromyces lactis strain GG799 from plasmid pSVB-Alc, recombinant enzyme expression in Escherichia coli
prochymosin cDNA, expressed as a NusA fusin protein in Escherichia coli, low level of milk clotting activity after activation at acidic pH
-
recombinant expression of the enzyme in Pichia pastoris resulting in production of chymosin and partially glycosylated chymosin
-
S351T mutant of prochymosin as fusion protein with the Aspergillus niger enzyme glucoamylase in Aspergillus niger var. awamori, insertion of a short peptide linker between the proteins with the sequence TDNST
-
the enzyme as a fusion with Tol-A-III protein is expressed in Escherichia coli BL21 (DE3) cells
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
oxidative refolding of solubilized enzyme obtained from inclusion bodies at pH 2 to obtain autoconversion of prochymosin to active chymosin
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
synthesis
-
use of chymosin to cleave a pro-chymosin derived fusion tag releasing native target proteins. After modification of the pro-chymosin fusion tag chymosin can remove this tag at more neutral pH 6.2, less prone to compromise the integrity of target proteins. Chymosin produces intact native target protein both at the level of small and large-scale preparations
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
the enzyme is used as milk coagulant in the cheese industry
food industry
-
the enzyme is used for the production of Reggianito cooked cheese
food industry
the enzyme is used industrially in cheese production
food industry
-
chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making
food industry
-
chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making
food industry
-
the enzyme plays an essential role in the coagulation of milk in the cheese industry
food industry
-
rabbit rennet is used as a remarkable ingredient of traditional cheese-making in the south-east region of Anatolia for a long time. Rabbit cheeses display better sensorial values and no extensive bitter taste occurs during the storage period. Recombinant rabbit chymosin could be an alternative agent for cheese making. Rabbit chymosin can be used to produce high quality cheeses with extended shelf-life
food industry
-
natural chymosin, derived from the stomachs of newborn farm animals, as well as its genetically engineered analogues are widely used in cheese production
food industry
recombinant camel chymosin can be used to make white soft cheese from camel milk, method development, optimization, and evaluation, overview
food industry
chymosin is used as an alternative to animal rennet. Animal rennet contains 3 genetic variants of chymosin: A, B, C (10-90%), and pepsin, which are aspartic proteases. Fermentation-produced recombinant chymosin is nature-identical calf chymosin produced through fermentation by an enzyme-expressing host microorganism. Recombinant chymosin covers a great percentage of the coagulant market. Fermentation-produced chymosin acts in a similar way to animal chymosin, but is much cheaper
food industry
calf chymosin/camel chymosin blend is used for production of Beyaz peynir, a white brined cheese. Determination of the best mixture of coagulant for Beyaz peynir, in terms of proteolysis, texture, and melting characteristics, overview
food industry
calf chymosin/camel chymosin blend is used for production of Beyaz peynir, a white brined cheese. Determination of the best mixture of coagulant for Beyaz peynir, in terms of proteolysis, texture, and melting characteristics, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mabrouk, S.S.; Amr, A.S.; Abdel-Fattah, A.F.
A rennin-like enzyme from Penicillium expansum
Agric. Biol. Chem.
40
419-420
1976
Penicillium expansum
-
brenda
Malak, C.A.A.; El Adab, I.F.G.A.; Vukashinovic, V.; Zalunin, I.A.; Timokhina, E.A.; Lavrenova, G.I.; Stepanov, V.M.
Buffalo (Bos buffali L.) chymosin purification and properties
Comp. Biochem. Physiol. B
113
57-62
1996
Bos taurus
brenda
Moir, D.; Mao, J.I.; Schumm, J.W.; Vovis, G.F.; Alford, B.L.; Taunton-Rigby, A.
Molecular cloning and characterization of double-stranded cDNA coding for bovine chymosin
Gene
19
127-138
1982
Bos taurus
brenda
Beppu, T.
The cloning and expression of chymosin (rennin) genes in microorganisms
Trends Biotechnol.
1
85-89
1983
Bos taurus
-
brenda
Gustchina, E.; Rumsh, L.; Ginodman, L.; Majer, P.; Andreeva, N.
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
FEBS Lett.
379
60-62
1996
Bos taurus
brenda
Kleinert, T.; Lange, I.; Roesicke, B.; Honig, A.; Schleusener, R.
Characterization and preparation of chymosin from calf rennet samples by means of isoelectric focusing
Acta Biotechnol.
8
367-375
1988
Bos taurus
-
brenda
Zayas, J.F.
Properties and quality characteristics of rennin extracted by ultrasound
Biotechnol. Bioeng.
29
969-975
1987
Bos taurus
brenda
Kawaguchi, Y.; Kosugi, S.; Sasaki, K.; Uozumi, T.; Beppu, T.
Production of chymosin in Escherichia coli cells and its enzymatic properties
Agric. Biol. Chem.
51
1871-1877
1987
Bos taurus
-
brenda
McCaman, M.T.; Andrews, W.H.; Files, J.G.
Enzymatic properties and processing of bovine prochymosin synthezised in Escherichia coli
J. Biotechnol.
2
177-190
1985
Bos taurus
-
brenda
Raap, J.; Kerling, K.E.T.; Vreeman, H.J.; Visser, S.
Peptide substrates for chymosin (rennin): conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular dichroism and secondary structure prediction
Arch. Biochem. Biophys.
221
117-124
1983
Bos taurus
brenda
Jensen, T.; Axelsen, N.H.; Foltmann, B.
Isolation and partial characterization of prochymosin and chymosin from cat
Biochim. Biophys. Acta
705
249-256
1982
Felis catus
brenda
Miyoshi, M.; Yoon, C.H.; Ibuki, F.; Kanamori, M.
The characterization of rennin action on kappa-casein using CM-cellulose
Agric. Biol. Chem.
40
347-352
1976
Bos taurus
-
brenda
Chang, W.J.; Takahashi, K.
The structure and function of acid proteases. III. Isolation and characterization of the active-site peptides from bovine rennin
J. Biochem.
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Bos taurus
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Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosin
Protein Eng.
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Bos taurus
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Akaeda, H.; Miura, H.; Mikami, M.
Studies on the rennin inhibitor in serum Part II: Inhibiting action on rennin coagulation by alpha2-macroglobulin
Nippon Nogeikagaku Kaishi
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Homo sapiens, Equus caballus, Ovis aries, Capra hircus, Oryctolagus cuniculus, Sus scrofa
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Foltmann, B.
Prochymosin and chymosin (prorennin and rennin)
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Bos taurus
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Azuma, N.; Kaminogawa, S.; Yamauchi, K.
Properties of glycomacropeptide and para-kappa-casein derived from human kappa-casein and comparison of human and bovine kappa-casein as to susceptibility to chymosin and pepsin
Agric. Biol. Chem.
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Homo sapiens, Bos taurus
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Abdel-Fattah, A.F.; Mabrouk, S.S.; El-Hawwary, N.M.
Production and some properties of rennin-like milk-clotting enzyme from Penicillium citrinum
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70
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1972
Penicillium citrinum
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Abdel-Fattah, A.F.; Abdel-Mohsen, S.I.; El-Aassar, S.A.
Purification and properties of rennin-like enzyme from Absidia cylindrospora
Zentralbl. Mikrobiol.
142
37-40
1987
Absidia cylindrospora
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brenda
Abdel-Mohsen, S.I.; El-Aassar, S.A.; Abdel-Fattah, A.F.
Partial purification of milk-clotting and caseinase enzymes, produced by Absidia cylindrospora, and isolation of rennin-like enzyme
Zentralbl. Mikrobiol.
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1987
Absidia cylindrospora
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brenda
Houen, G.; Madsen, M.T.; Harlow, K.W.; Lonblad, P.; Foltmann, B.
The primary structure and enzymic properties of porcine prochymosin and chymosin
Int. J. Biochem. Cell Biol.
28
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1996
Sus scrofa
brenda
Pitts, J.E.; Quinn, D.; Uusitalo, J.; Penttilae, M.
Protein engineering of chymosin and expression in Trichoderma reesei
Food Biotechnol.
19
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1991
Bos taurus
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Strop, P.; Sedlacek, J.; Stys, J.; Kaderabkova, Z.; Blaha, I.; Pavlickova, L.; Pohl, J.; Fabry, M.; Kostka, V.; Newman, M.; Frazao, C.; Shearer, A.; Tickle, I.J.; Blundell, T.L.
Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin
Biochemistry
29
9863-9871
1990
Bos taurus
brenda
Pitts, J.E.; Uusitalo, J.M.; Mantafounis, D.; Nugent, P.G.; Quinn, D.D.; Orprayoon, P.; Penttilae, M.E.
Expression and characterisation of chymosin pH optima mutants produced in Trichoderma reesei
J. Biotechnol.
28
69-83
1993
Bos taurus
brenda
Nugent, P.G.; Albert, A.; Orprayoon, P.; Wilsher, J.; Pitts, J.E.; Blundell, T.L.; Dhanaraj, V.
Protein engineering loops in aspartic proteinases: site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin
Protein Eng.
9
885-893
1996
Bos taurus
brenda
Mantafounis, D.; Pitts, J.
Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis
Protein Eng.
3
605-609
1990
Bos taurus
brenda
Gustchina, E.A.; Majer, P.; Rumsh, L.D.; Ginodman, L.M.; Andreeva, N.S.
Post X-ray crystallographic studies of chymosin specificity. The role of histidine-proline cluster of kappa-casein in catalytic reactions
Adv. Exp. Med. Biol.
436
179-184
1998
Bos taurus
brenda
Beldarrain, A.; Acosta, N.; Montesinos, R.; Mata, M.; Cremata, J.
Characterization of Mucor pusillus rennin expressed in Pichia pastoris: enzymic, spectroscopic and calorimetric studies
Biotechnol. Appl. Biochem.
31
77-84
2000
Rhizomucor pusillus
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brenda
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
Camelus dromedarius, Bos taurus
brenda
Kageyama, T.
Role of S1 loop residues in the substrate specificities of pepsin A and chymosin
Biochemistry
43
15122-15130
2004
Callithrix jacchus
brenda
Starovoitova, V.V.; Velichko, T.I.; Baratova, L.A.; Filippova, I.Y.; Lavrenova, G.I.
A comparative study of functional properties of calf chymosin and its recombinant forms
Biochemistry (Moscow)
71
320-324
2006
Bos taurus
brenda
Huppertz, T.; Uniacke, T.; Kelly, A.L.; Fox, P.F.
Inhibition of the proteolytic activity of indigenous plasmin or exogenous chymosin and pepsin in bovine milk by blood serum
Int. dairy J.
16
691-696
2006
Bos taurus
-
brenda
Moschopoulou, E.E.; Kandarakis, I.G.; Alichanidis, E.; Anifantakis, E.M.
Purification and characterization of chymosin and pepsin from kid
J. Dairy Res.
73
49-57
2006
Bos taurus
brenda
Kumar, A.; Sharma, J.; Mohanty, A.K.; Grover, S.; Batish, V.K.
Purification and characterization of milk clotting enzyme from goat (Capra hircus)
Comp. Biochem. Physiol. B
145
108-113
2006
Capra hircus (Q5VK60), Capra hircus
brenda
Kumar, A.; Sharma, J.; Grover, S.; Mohanty, A.K.; Batish, V.K.
Molecular cloning and expression of goat (Capra hircus) prochymosin in E. coli
Food Biotechnol.
21
57-69
2007
Capra hircus
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brenda
Molle, D.; Jean, K.; Guyomarch, F.
Chymosin sensitivity of the heat-induced serum protein aggregates isolated from skim milk
Int. Dairy J.
16
1435-1441
2006
Bos taurus
-
brenda
Bansal, N.; Fox, P.F.; McSweeney, P.L.
Aggregation of rennet-altered casein micelles at low temperatures
J. Agric. Food Chem.
55
3120-3126
2007
Bos taurus
brenda
Renan, M.; Guyomarch, F.; Chatriot, M.; Gamerre, V.; Famelart, M.H.
Limited enzymatic treatment of skim milk using chymosin affects the micelle/serum distribution of the heat-induced whey protein/kappa-casein aggregates
J. Agric. Food Chem.
55
6736-6745
2007
Bos taurus
brenda
van den Brink, H.J.; Petersen, S.G.; Rahbek-Nielsen, H.; Hellmuth, K.; Harboe, M.
Increased production of chymosin by glycosylation
J. Biotechnol.
125
304-310
2006
Bos taurus
brenda
Reh, G.; Spelzini, D.; Tubio, G.; Pico, G.; Farruggia, B.
Partition features and renaturation enhancement of chymosin in aqueous two-phase systems
J. Chromatogr. B
860
98-105
2007
Bos taurus
brenda
Vallejo, J.A.; Ageitos, J.M.; Poza, M.; Villa, T.G.
Cloning and expression of buffalo active chymosin in Pichia pastoris
J. Agric. Food Chem.
56
10606-10610
2008
Bubalus bubalis (Q9N1p5), Bubalus bubalis
brenda
Palmer, D.S.; Christensen, A.U.; Srensen, J.; Celik, L.; Qvist, K.B.; Schiott, B.
Bovine chymosin: a computational study of recognition and binding of bovine kappa-casein
Biochemistry
49
2563-2573
2010
Bos taurus
brenda
Hidalgo, M.E.; Pires, M.S.; Risso, P.H.
A study on bovine kappa-casein aggregation after the enzymatic action of chymosin
Colloids Surf. B Biointerfaces
76
556-563
2010
Bos taurus
brenda
Kumar, A.; Grover, S.; Sharma, J.; Batish, V.K.
Chymosin and other milk coagulants: sources and biotechnological interventions
Crit. Rev. Biotechnol.
30
243-258
2010
Bos taurus
brenda
Kageyama, H.; Ueda, H.; Tezuka, T.; Ogasawara, A.; Narita, Y.; Kageyama, T.; Ichinose, M.
Differences in the P1' substrate specificities of pepsin A and chymosin
J. Biochem.
147
167-174
2010
Bos taurus (P00794), Bos taurus
brenda
Justesen, S.F.; Lamberth, K.; Nielsen, L.L.; Schafer-Nielsen, C.; Buus, S.
Recombinant chymosin used for exact and complete removal of a prochymosin derived fusion tag releasing intact native target protein
Protein Sci.
18
1023-1032
2009
Bos taurus
brenda
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
Camelus dromedarius (Q9GK11), Bos taurus (P00794), Bos taurus
brenda
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)
brenda
Sun, Q.; Wang, X.P.; Yan, Q.J.; Chen, W.; Jiang, Z.Q.
Purification and characterization of a chymosin from Rhizopus microsporus var. rhizopodiformis
Appl. Biochem. Biotechnol.
174
174-185
2014
Rhizopus microsporus, Rhizopus microsporus F518
brenda
Eskandari, M.; Hosseini, A.; Alasvand Zarasvand, S.; Aminlari, M.
Cloning, expression, purification and refolding of caprine prochymosin
Food Biotechnol.
26
143-153
2012
Capra hircus (Q5VK60)
-
brenda
Bijl, E.; van Valenberg, H.; Sikkes, S.; Jumelet, S.; Sala, G.; Olieman, K.; van Hooijdonk, T.; Huppertz, T.
Chymosin-induced hydrolysis of caseins: Influence of degree of phosphorylation of alpha-s1-casein and genetic variants of beta-casein
Int. Dairy J.
39
215-221
2014
Bos taurus
-
brenda
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
brenda
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, Bos taurus
brenda
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
Camelus dromedarius, Bos taurus
brenda
Noseda, D.G.; Blasco, M.; Recupero, M.; Galvagno, M.A.
Bioprocess and downstream optimization of recombinant bovine chymosin B in Pichia (Komagataella) pastoris under methanol-inducible AOXI promoter
Protein Expr. Purif.
104
85-91
2014
Bos taurus
brenda
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)
brenda
Belenkaya, S.; Rudometov, A.; Shcherbakov, D.; Balabova, D.; Kriger, A.; Belov, A.; Koval, A.; Elchaninov, V.
Biochemical properties of recombinant chymosin in alpaca (Vicugna pacos L.)
Appl. Biochem. Microbiol.
54
569-576
2018
Vicugna pacos, Bos taurus
-
brenda
Rayanatou, I.A.; Mahamadou, E.G.; Garric, G.; Harel-Oger, M.; Leduc, A.; Jardin, J.; Briard-Bion, V.; Cauty, C.; Adakal, H.; Grongnet, J.F.; Gaucheron, F.
Physico-chemical characterization of dairy gel obtained by a proteolytic extract from Calotropis procera - A comparison with chymosin
Food Chem.
232
405-412
2017
Bos taurus
brenda
Wei, Z.Y.; Zhang, Y.Y.; Wang, Y.P.; Fan, M.X.; Zhong, X.F.; Xu, N.; Lin, F.; Xing, S.C.
Production of bioactive recombinant bovine chymosin in tobacco plants
Int. J. Mol. Sci.
17
E624
2016
Bos taurus
brenda
Rolet-Repecaud, O.; Arnould, C.; Dupont, D.; Gavoye, S.; Beuvier, E.; Achilleos, C.
Development and evaluation of a monoclonal antibody-based inhibition ELISA for the quantification of chymosin in solution
J. Agric. Food Chem.
63
4799-4804
2015
Bos taurus
brenda
Ansari, S.M.; Coletta, A.; Kirkeby Skeby, K.; Sorensen, J.; Schiott, B.; Palmer, D.S.
Allosteric-activation mechanism of bovine chymosin revealed by bias-exchange metadynamics and molecular dynamics simulations
J. Phys. Chem. B
120
10453-10462
2016
Bos taurus (P00794), Bos taurus
brenda
Tyagi, A.; Kumar, A.; Yadav, A.; Chandola Saklani, A.; Grover, S.; Batish, V.
Functional expression of recombinant goat chymosin in Pichia pastoris bioreactor cultures A commercially viable alternate
LWT-Food Sci. Technol.
69
217-224
2016
Capra hircus (Q5VK60)
-
brenda
Leite Junior, B.; Tribst, A.; Cristianini, M.
The effect of high pressure processing on recombinant chymosin, bovine rennet and porcine pepsin Influence on the proteolytic and milk-clotting activities and on milk-clotting characteristics
LWT-Food Sci. Technol.
76
351-360
2017
Bos taurus
-
brenda
Espinoza-Molina, J.A.; Acosta-Muniz, C.H.; Sepulveda, D.R.; Zamudio-Flores, P.B.; Rios-Velasco, C.
Codon optimization of the "Bos taurus Chymosin" gene for the production of recombinant chymosin in Pichia pastoris
Mol. Biotechnol.
58
657-664
2016
Bos taurus
brenda
Ulusu, Y.; Sentuerk, S.B.; Kudug, H.; Goekce, I.
Expression, purification, and characterization of bovine chymosin enzyme using an inducible pTOLT system
Prep. Biochem. Biotechnol.
46
596-601
2016
Bos taurus
brenda
Liu, W.G.; Wang, Y.P.; Zhang, Z.J.; Wang, M.; Lv, Q.X.; Liu, H.W.; Meng, L.C.; Lu, M.
Generation and characterization of caprine chymosin in corn seed
Protein Expr. Purif.
135
78-82
2017
Capra hircus (Q5VK60)
brenda
Ersoez, F.; Inan, M.
Large-scale production of yak (Bos grunniens) chymosin A in Pichia pastoris
Protein Expr. Purif.
154
126-133
2019
Bos grunniens (M4LK61), Bos grunniens
brenda
Ansari, S.M.; Sorensen, J.; Schiott, B.; Palmer, D.S.
On the effect of mutations in bovine or camel chymosin on the thermodynamics of binding kappa-caseins
Proteins
86
75-87
2018
Camelus dromedarius (Q9GK11), Bos taurus (P00794), Bos taurus
brenda
Belenkaya, S.V.; Bondar, A.A.; Kurgina, T.A.; Elchaninov, V.V.; Bakulina, A.Y.; Rukhlova, E.A.; Lavrik, O.I.; Ilyichev, A.A.; Shcherbakov, D.N.
Characterization of the Altai maral chymosin gene, production of a chymosin recombinant analog in the prokaryotic expression system, and analysis of its several biochemical properties
Biochemistry (Moscow)
85
781-791
2020
Cervus canadensis sibiricus (A0A7D3Q7Y7)
brenda
Murashkin, D.E.; Belenkaya, S.V.; Bondar, A.A.; Elchaninov, V.V.; Shcherbakov, D.N.
Analysis of some biochemical properties of recombinant siberian roe deer (Capreolus pygargus) chymosin obtained in the mammalian cell culture (CHO-K1)
Biochemistry (Moscow)
88
1284-1295
2023
Capreolus pygargus
brenda
Camin, F.; Bontempo, L.; Ziller, L.; Franceschi, P.; Molteni, A.; Corbella, R.; Verga, I.
Assessing the authenticity of animal rennet using delta15N analysis of chymosin
Food Chem.
293
545-549
2019
Bos taurus (P00794)
brenda
Al-Zoreky, N.S.; Almathen, F.S.
Using recombinant camel chymosin to make white soft cheese from camel milk
Food Chem.
337
127994
2021
Camelus dromedarius (Q9GK11)
brenda
Balabova, D.V.; Belash, E.A.; Belenkaya, S.V.; Shcherbakov, D.N.; Belov, A.N.; Koval, A.D.; Mironova, A.V.; Bondar, A.A.; Volosnikova, E.A.; Arkhipov, S.G.; Sokolova, O.O.; Chirkova, V.Y.; Elchaninov, V.V.
Biochemical properties of a promising milk-clotting enzyme, moose (Alces alces) recombinant chymosin
Foods
12
3772
2023
Alces alces alces (A0A8E3Z7B9)
brenda
Gumus, P.; Hayaloglu, A.A.
Effects of blends of camel and calf chymosin on proteolysis, residual coagulant activity, microstructure, and sensory characteristics of Beyaz peynir
J. Dairy Sci.
102
5945-5956
2019
Bos taurus (P00794), Camelus dromedarius (Q9GK11)
brenda
Azizi-Dargahlou, S.; Pouresmaeil, M.; Ahmadabadi, M.
Tobacco plant a novel and promising heterologous bioreactor for the production of recombinant bovine chymosin
Mol. Biotechnol.
66
2596-2605
2024
Bos taurus (P00794)
brenda
Chen, C.C.; Chen, L.Y.; Li, W.T.; Chang, K.L.; Kuo, M.I.; Chen, C.J.; Hsieh, J.F.
Influence of chymosin on physicochemical and hydrolysis characteristics of casein micelles and individual caseins
Nanomaterials (Basel)
11
2594
2021
Bos taurus (P00794)
brenda
Ali Hanoglu, S.; Ektiren, D.; Karaaslan, M.
Recombinant expression and characterization of Oryctolagus cuniculus chymosin in Komagataella phaffii (Pichia pastoris)
Protein Expr. Purif.
183
105874
2021
Oryctolagus cuniculus
brenda
Mbye, M.; Mohamed, H.; Raziq, A.; Kamal-Eldin, A.
The effects of camel chymosin and Withania coagulans extract on camel and bovine milk cheeses
Sci. Rep.
11
13573
2021
Camelus dromedarius (Q9GK11)
brenda
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