3.4.23.4: chymosin
This is an abbreviated version!
For detailed information about chymosin, go to the full flat file.
Word Map on EC 3.4.23.4
-
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
- 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
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
CHY-MAX, CHY-MAX 200, chymase, chymosin, chymosin A, chymosin B, CYM, EC 3.4.4.3, More, Preprorennin, prochymosin, rCH, rennin
ECTree
3.4.23.4 chymosinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.23.4 - chymosin
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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
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-A-A-p-nitroanilide + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-pnA + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
AFPLEFEREL + H2O
AFPLEF + EREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
AFPLEFFREL + H2O
AFPLEF + FREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
AFPLEFIREL + H2O
AFPLEF + IREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
AFPLEFKREL + H2O
AFPLEF + KREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
basic FGF 110-118 + H2O
?
-
parent peptide and Leu115 and Lys115 variants respectively as substrate
-
-
?
bovine kappa-casein residues 97-112 + H2O
?
-
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
-
-
?
dynorphin A 1-7e + H2O
?
-
Ala3Phe7 and ILe3Lys5Phe7 variants respectively as substrate
-
-
?
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
His-Pro-His-Pro-His-Leu-Ser-Phe-Phe(NO2)-Ala-Ile-Pro-Pro-Lys-Lys + H2O
?
-
-
-
-
?
kappa-casein + H2O
para-kappa-casein + glycopeptide
cleavage between Phe105-Met106
-
-
?
kappa-casein + H2O
para-kappa-casein + macropeptide
-
kappa-casein is the primary substrate for the chymosin action
-
-
?
L-S-F-M-A-I-P-NH2 + H2O
?
-
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
-
-
?
Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Leu-Ser-Phe-Met-Ala-O-methyl ester + H2O
Leu-Ser-Phe + Met-Ala-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Lys-Pro-Leu-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Leu-Glu-Phe + Phe(NO2)-Arg-Leu
-
-
-
?
NT/NMN 142-151 + H2O
?
-
parent peptide, Glu148 and Phe148 variants respectively as substrate
-
-
?
o-aminobenzoyl-Ala-Ala-Phe-Phe-Ala-Ala-NH-C6H4NO2 + H2O
o-aminobenzoyl-Ala-Ala-Phe + Phe-Ala-Ala-NHC6H4NO2
-
-
-
?
o-aminobenzoyl-Ala-Ala-Phe-Phe-NH-C6H4-NO2 + H2O
o-aminobenzoyl-Ala-Ala-Phe + Phe-NH-C6H4-NO2
-
-
-
?
POm C165-174 + H2O
?
-
parent peptide and Glu171 variant respectively as substrate
-
-
?
Pro-His-Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Pro-His-Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Ser-Phe + Met-Ala-Ile-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Substance P + H2O
?
-
parent peptide and Lys8 variant respectively as substrate
-
-
?
undecapeptide analogue to chymosin sensitive region of bovine kappa casein
?
-
synthetic substrate
-
-
?
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
?
-
synthetic substrate
-
-
?
undecapeptide analogue to chymosin sensitive region of camel kappa-casein + H2O
?
-
-
-
-
?
YGISSKFCE + H2O
YGISSKF + L-Cys-L-Glu
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFfE + H2O
YGISSKF + FE
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFHE + H2O
YGISSKF + His-Glu
-
modified peptide based on prochymosin sequence
51% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFIE + H2O
YGISSKF + Ile-Glu
-
modified peptide based on prochymosin sequence
54% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFKE + H2O
YGISSKF + Lys-Glu
-
modified peptide based on prochymosin sequence
33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFLE + H2O
YGISSKF + L-Leu-L-Glu
-
modified peptide based on prochymosin sequence
42% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFME + H2O
YGISSKF + L-Met-L-Glu
-
modified peptide based on prochymosin sequence
52% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFNE + H2O
YGISSKF + L-Asn-L-Glu
-
modified peptide based on prochymosin sequence
33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFRE + H2O
YGISSKF + Arg-Glu
-
modified peptide based on prochymosin sequence
59% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFVE + H2O
YGISSKF + Val-Glu
-
modified peptide based on prochymosin sequence
36% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFWE + H2O
YGISSKF + Trp-Glu
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFYE + H2O
YGISSKF + L-Tyr-L-Glu
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
alpha-casein + H2O
?
-
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
-
-
?
alpha-casein + H2O
?
-
alpha-casein is hydrolyzed extensively
-
-
?
beta-casein + H2O
?
-
in sodium caseinate solutions, more than 10% more beta-casein A2 is degraded compared with beta-casein A1 and B at 50% casein degradation
-
-
?
bovine kappa-casein + H2O
?
-
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
-
-
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
the enzyme cleaves the Phe105-Met106 bond of kappa-casein
-
-
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
the enzyme cleaves the Phe105-Met106 bond of kappa-casein
-
-
?
casein + H2O
?
-
the enzyme breaks the bond between Phe-105 and Met-106 in the casein and initiates the coagulation of milk
-
-
?
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
-
part of the bovine kappa-casein sequence
-
?
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
-
part of the bovine kappa-casein sequence
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
36869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36893, 36894
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
-
-
?
kappa-casein + H2O
?
-
the bond Phe105-Met106 is the main hydrolyzed bond by the enzyme
-
-
?
kappa-casein + H2O
?
the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
casein macropeptide + para-kappa-casein
-
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
-
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
part of the bovine kappa-casein sequence
-
?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
part of the bovine kappa-casein sequence
-
?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
-
-
-
?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
-
-
-
?
milk + H2O
?
-
the maximum increase on milk-clotting activity is 10% for recombinant chymosin at 212MPa/5 min/10°C
-
-
?
additional information
?
-
in acidic conditions, the inactive proenzyme converts to the active form by autocatalytically cleavage of prosequence
-
-
?
additional information
?
-
-
in acidic conditions, the inactive proenzyme converts to the active form by autocatalytically cleavage of prosequence
-
-
?
additional information
?
-
bovine chymosin is a poor coagulant for camel milk
-
-
?
additional information
?
-
-
bovine chymosin is a poor coagulant for camel milk
-
-
?
additional information
?
-
-
in the process of milk coagulation under the action of chymosin, alpha- and beta-caseins are not hydrolyzed
-
-
?
additional information
?
-
does not cleave alpha-casein and beta-casein
-
-
?
additional information
?
-
camel chymosin is also a good coagulant for bovine milk
-
-
?
additional information
?
-
-
in the process of milk coagulation under the action of chymosin, alpha- and beta-caseins are not hydrolyzed
-
-
?
