Information on EC 3.4.23.4 - chymosin:
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The lowest common taxonomy group for this enzyme is: Opisthokonta

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EC NUMBERCOMMENTARY
3.4.23.4-

RECOMMENDED NAMEGeneOntology No.
chymosinGO:0030602

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.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
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of peptide bond--endopeptidase; peptides, endopeptidase-

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
No entries in this field

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
chymase----
chymosinBubalus bubalisQ9N1p5-698398
chymosin ABos taurus-allelic form708236
chymosin BBos taurus-allelic form708236
Preprorennin----
prochymosinCapra hircusQ5VK60inactive precursor686199
prochymosinCapra hircus-cDNA predicted to code for 365 amino acids with a 42 amino acids long pro-region686839
prochymosinBos taurus-inactive687952
rennin----
EC 3.4.4.3--formerly-
additional informationCapra hircusQ5VK60acid protease, major component of rennet (milk clotting enzyme)686199

CAS REGISTRY NUMBERCOMMENTARY
9001-98-3-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Absidia cylindrosporasimilarar enzyme36885, 36886--Manually annotated by BRENDA team
Bos taurus-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, 710493--Manually annotated by BRENDA team
Bos taurus-708952, 717696P00794UniProtManually annotated by BRENDA team
Bos tauruschymosin derived as commercial enzyme preparation (Maxiren) from a genetically modified yeast Kluyveromyces lactic687104, 687229, 687241--Manually annotated by BRENDA team
Bos taurususe of a synthetic gene that encodes a protein identical to bovine prochymosin687865--Manually annotated by BRENDA team
Bubalus bubalis-698398Q9N1p5UniProtManually annotated by BRENDA team
Callithrix jacchus-667593--Manually annotated by BRENDA team
Camelus dromedarius-667435--Manually annotated by BRENDA team
Camelus dromedarius-717696Q9GK11UniProtManually annotated by BRENDA team
Capra hircus-36881, 686839--Manually annotated by BRENDA team
Capra hircussynthetic construct of prochymosin mRNA; enzyme secretion is maximal during the first days after birth, enzyme level declines thereafter and chymosin in replaced by pepsin686199Q5VK60UniProtManually annotated by BRENDA team
Equus caballus-36881--Manually annotated by BRENDA team
Felis catussimilar enzyme36877--Manually annotated by BRENDA team
Homo sapiens-36881, 36883--Manually annotated by BRENDA team
Oryctolagus cuniculus-36881--Manually annotated by BRENDA team
Ovis aries-36881--Manually annotated by BRENDA team
Penicillium citrinumsimilar enzyme36884--Manually annotated by BRENDA team
Penicillium expansumsimilar enzyme30594--Manually annotated by BRENDA team
Rhizomucor pusillus-650661--Manually annotated by BRENDA team
Sus scrofa-36881, 36888--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionBos taurus-chymosin, an aspartic protease, is the main enzymatic component of calf rennet708236

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O?
show the reaction diagram		Bos taurus-low molecular weight, fluorogenic peptide substrate667763--?
Abz-A-A-F-F-A-A-p-nitroanilide + H2O?
show the reaction diagram		Bos taurus-low molecular weight, fluorogenic peptide substrate667763--?
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O?
show the reaction diagram		Bos taurus-low molecular weight, fluorogenic peptide substrate667763--?
Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine + H2O?
show the reaction diagram		Bos taurus-low molecular weight, fluorogenic peptide substrate667763--?
Abz-A-A-F-F-pnA + H2O?
show the reaction diagram		Bos taurus-low molecular weight, fluorogenic peptide substrate667763--?
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O?
show the reaction diagram		Bos taurus-low molecular weight, fluorogenic peptide substrate667763--?
acid denatured hemoglobin + H2O?
show the reaction diagram		Bos taurus--35015--?
acid denatured hemoglobin + H2O?
show the reaction diagram		Felis catus--36877--?
AFPLEFEREL + H2OAFPLEF + EREL
show the reaction diagram		Bos taurusP00794modified peptide substrate based on residues 165-174 of proopiomelanocortin708952--?
AFPLEFFREL + H2OAFPLEF + FREL
show the reaction diagram		Bos taurusP00794modified peptide substrate based on residues 165-174 of proopiomelanocortin708952--?
AFPLEFIREL + H2OAFPLEF + IREL
show the reaction diagram		Bos taurusP00794modified peptide substrate based on residues 165-174 of proopiomelanocortin708952--?
AFPLEFKREL + H2OAFPLEF + KREL
show the reaction diagram		Bos taurusP00794modified peptide substrate based on residues 165-174 of proopiomelanocortin708952--?
alpha-casein + H2O?
show the reaction diagram		Bos taurus--708236--?
alphaS-casein + H2O?
show the reaction diagram		Bos taurus, Camelus dromedarius--667435--?
basic FGF 110-118 + H2O?
show the reaction diagram		Callithrix jacchus-parent peptide and Leu115 and Lys115 variants respectively as substrate667593--?
beta-casein + H2O?
show the reaction diagram		Bos taurus--667435, 708236--?
beta-casein + H2O?
show the reaction diagram		Camelus dromedarius--667435--?
beta-casein + H2O?
show the reaction diagram		Bos taurus-occurs during the long period of renneting687229--?
beta-chain of proteolytic insulin + H2O?
show the reaction diagram		Bos taurus-general proteolytic activity36882--?
bovine kappa-casein + H2O?
show the reaction diagram		Bos taurus-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-chymosin708213--?
bovine kappa-casein residues 97-112 + H2O?
show the reaction diagram		Bos taurus-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 simulations707523--?
casein + H2O?
show the reaction diagram		Bos taurus--668957, 669642--?
dynorphin A 1-7e + H2O?
show the reaction diagram		Callithrix jacchus-Ala3Phe7 and ILe3Lys5Phe7 variants respectively as substrate667593--?
fluorescein thiocarbamoyl-kappa-casein + H2O?
show the reaction diagram		Bubalus bubalisQ9N1p5-698398--?
His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2OHis-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36871-36871?
His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2OHis-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36894-36894?
His-Pro-His-Pro-His-Leu-Ser-Phe-Phe(NO2)-Ala-Ile-Pro-Pro-Lys-Lys + H2O?
show the reaction diagram		Bos taurus--36880, 36892--?
HPHPHLSFMAIPPKK + H2O?
show the reaction diagram		Bos taurus--708236--?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Homo sapiens, Sus scrofa-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881--?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Bos taurus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636869, 36870, 36872, 36873, 36874, 36875, 36876, 36879, 36880, 36882--?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Oryctolagus cuniculus, Ovis aries-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881--?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Felis catus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636877--?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Capra hircus, Equus caballus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881--?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Homo sapiens-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636883p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction36883?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Bos taurus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636878p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction36878?
kappa-casein + H2Op-kappa-casein + glycomacropeptide
show the reaction diagram		Bos taurus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636883p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction36883?
kappa-casein + H2O?
show the reaction diagram		Capra hircusQ5VK60-686199--?
kappa-casein + H2O?
show the reaction diagram		Bubalus bubalisQ9N1p5-698398--?
kappa-casein + H2O?
show the reaction diagram		Bos taurus--717696--?
kappa-casein + H2O?
show the reaction diagram		Camelus dromedariusQ9GK11-717696--?
kappa-casein + H2O?
show the reaction diagram		Homo sapiens-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881, 36883---
kappa-casein + H2O?
show the reaction diagram		Sus scrofa-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881---
kappa-casein + H2O?
show the reaction diagram		Bos taurus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36893, 36894---
kappa-casein + H2O?
show the reaction diagram		Oryctolagus cuniculus, Ovis aries-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881---
kappa-casein + H2O?
show the reaction diagram		Felis catus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636877---
kappa-casein + H2O?
show the reaction diagram		Capra hircus, Equus caballus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881---
kappa-casein + H2O?
show the reaction diagram		Penicillium citrinum-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636884---
kappa-casein + H2O?
show the reaction diagram		Penicillium expansum-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10630594---
kappa-casein + H2O?
show the reaction diagram		Absidia cylindrospora-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636885, 36886---
kappa-casein + H2O?
show the reaction diagram		Bos taurus-cleaves a single bond between phenylalanine 105 and methionine 106687865--?
kappa-casein + H2O?
show the reaction diagram		Capra hircusQ5VK60cleaves a single bond between phenylalanine 105 and methionine 106686199--?
kappa-casein + H2O?
show the reaction diagram		Bos taurus-involved in milk clotting687952--?
kappa-casein + H2O?
show the reaction diagram		Capra hircus-involved in milk clotting686839--?
kappa-casein + H2Ocasein macropeptide + para-kappa-casein
show the reaction diagram		Bos taurus--687104, 687229--?
kappa-casein + H2Ocasein macropeptide + para-kappa-casein
show the reaction diagram		Bos taurus-cleaves a single bond between phenylalanine 105 and methionine 106687104, 687229--?
kappa-casein + H2Ocaseinmacropeptide + para-kappa-casein
show the reaction diagram		Bos taurus-cleaves a single bond between phenylalanine 105 and methionine 106687241--?
kappa-casein + H2Opara-kappa-casein + macropeptide
show the reaction diagram		Bos taurus-kappa-casein is the primary substrate for the chymosin action708236--?
L-S-F-M-A-I-P-NH2 + H2O?
show the reaction diagram		Bos taurus-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 chymosin667763--?
Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe + H2O?
show the reaction diagram		Bos taurus--36880, 36892--?
Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2OLeu-Ser-Phe + Met-Ala-Ile-O-methyl ester
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36876-36876?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2OLeu-Ser-Phe + Met-Ala-Ile-Pro + NH3
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36871-36871?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2OLeu-Ser-Phe + Met-Ala-Ile-Pro + NH3
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36894-36894?
Leu-Ser-Phe-Met-Ala-O-methyl ester + H2OLeu-Ser-Phe + Met-Ala-O-methyl ester
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36876-36876?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2OLys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
show the reaction diagram		Bos taurus--36889-36889?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2OLys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
show the reaction diagram		Bos taurus--36891-36891?
Lys-Pro-Leu-Glu-Phe-Phe(NO2)-Arg-Leu + H2OLys-Pro-Leu-Glu-Phe + Phe(NO2)-Arg-Leu
show the reaction diagram		Bos taurus--36890-36890?
NT/NMN 142-151 + H2O?
show the reaction diagram		Callithrix jacchus-parent peptide, Glu148 and Phe148 variants respectively as substrate667593--?
o-aminobenzoyl-Ala-Ala-Phe-Phe-Ala-Ala-NH-C6H4NO2 + H2Oo-aminobenzoyl-Ala-Ala-Phe + Phe-Ala-Ala-NHC6H4NO2
show the reaction diagram		Bos taurus--35015-35015?
o-aminobenzoyl-Ala-Ala-Phe-Phe-NH-C6H4-NO2 + H2Oo-aminobenzoyl-Ala-Ala-Phe + Phe-NH-C6H4-NO2
show the reaction diagram		Bos taurus--35015-35015?
POm C165-174 + H2O?
show the reaction diagram		Callithrix jacchus-parent peptide and Glu171 variant respectively as substrate667593--?
Pro-His-Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2OPro-His-Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36876-36876?
Ser-Phe-Met-Ala-Ile-O-methyl ester + H2OSer-Phe + Met-Ala-Ile-O-methyl ester
show the reaction diagram		Bos taurus-part of the bovine kappa-casein sequence36876-36876?
Substance P + H2O?
show the reaction diagram		Callithrix jacchus-parent peptide and Lys8 variant respectively as substrate667593--?
undecapeptide analogue to chymosin sensitive region of bovine kappa casein?
show the reaction diagram		Bos taurus-synthetic substrate667435--?
undecapeptide analogue to chymosin sensitive region of bovine kappa-casein?
show the reaction diagram		Camelus dromedarius-synthetic substrate667435--?
undecapeptide analogue to chymosin sensitive region of camel kappa casein?
show the reaction diagram		Bos taurus-synthetic substrate667435--?
undecapeptide analogue to chymosin sensitive region of camel kappa-casein?
show the reaction diagram		Camelus dromedarius-synthetic substrate667435--?
YGISSKFCE + H2OYGISSKF + CE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence710493100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFfE + H2OYGISSKF + FE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence710493100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFHE + H2OYGISSKF + HE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049351% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFIE + H2OYGISSKF + IE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049354% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFKE + H2OYGISSKF + KE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049333% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFLE + H2OYGISSKF + LE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049342% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFME + H2OYGISSKF + ME
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049352% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFNE + H2OYGISSKF + NE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049333% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFRE + H2OYGISSKF + RE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049359% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFVE + H2OYGISSKF + VE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence71049336% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFWE + H2OYGISSKF + WE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence710493100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?
YGISSKFYE + H2OYGISSKF + YE
show the reaction diagram		Bos taurus-modified peptide based on prochymosin sequence710493100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h-?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
kappa-casein + H2O?
show the reaction diagram		Homo sapiens-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881, 36883--
kappa-casein + H2O?
show the reaction diagram		Sus scrofa-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881--
kappa-casein + H2O?
show the reaction diagram		Bos taurus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36893, 36894--
kappa-casein + H2O?
show the reaction diagram		Oryctolagus cuniculus, Ovis aries-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881--
kappa-casein + H2O?
show the reaction diagram		Felis catus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636877--
kappa-casein + H2O?
show the reaction diagram		Capra hircus, Equus caballus-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636881--
kappa-casein + H2O?
show the reaction diagram		Penicillium citrinum-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636884--
kappa-casein + H2O?
show the reaction diagram		Penicillium expansum-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10630594--
kappa-casein + H2O?
show the reaction diagram		Absidia cylindrospora-cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 10636885, 36886--
kappa-casein + H2O?
show the reaction diagram		Bos taurus-cleaves a single bond between phenylalanine 105 and methionine 106687865--
kappa-casein + H2O?
show the reaction diagram		Capra hircusQ5VK60cleaves a single bond between phenylalanine 105 and methionine 106686199--
kappa-casein + H2O?
show the reaction diagram		Bos taurus-involved in milk clotting687952--
kappa-casein + H2O?
show the reaction diagram		Capra hircus-involved in milk clotting686839--
kappa-casein + H2Ocasein macropeptide + para-kappa-casein
show the reaction diagram		Bos taurus-cleaves a single bond between phenylalanine 105 and methionine 106687104, 687229--
kappa-casein + H2Ocaseinmacropeptide + para-kappa-casein
show the reaction diagram		Bos taurus-cleaves a single bond between phenylalanine 105 and methionine 106687241--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ca2+Bos taurus-stimulation of milk clotting activity36874

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1-2-Epoxy-3(p-nitrophenoxy)propaneBos taurus--36879 2D-image
alpha2-MacroglobulinCapra hircus, Equus caballus, Homo sapiens, Oryctolagus cuniculus, Ovis aries, Sus scrofa--36881-
Blood serumBos taurus-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 substance668957-
Diazoacetylnorleucine methyl esterBos taurus-in presence of Cu2+36879 2D-image
PepstatinBos taurus--36875 2D-image
PepstatinBos taurus-inhibits recombinant and transgenic chymosin less efficiently than the native enzyme667763 2D-image
pepstatin ABos taurus--687229 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
His-Pro-His-Pro-His-NH2Bos taurus-stimulation, part of kappa-casein36871 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0056-Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by recombinant chymosin; hydrolysis by transgenic chymosin667763 2D-image
0.007-Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
0.004-Abz-A-A-F-F-A-A-p-nitroanilideBos taurus-hydrolysis by calf chymosin667763 2D-image
0.0022-Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
0.0035-Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by recombinant chymosin667763 2D-image
0.018-Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by transgenic chymosin667763 2D-image
0.003-Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
0.0018-Abz-A-A-F-F-p-nitroanilideBos taurus-hydrolysis by calf chymosin667763 2D-image
0.0018-Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
0.0021-Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by recombinant chymosin667763 2D-image
0.0078-Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by transgenic chymosin667763 2D-image
3.3-AFPLEFERELBos taurus-pH 4.0, 37°C708952-
0.041-AFPLEFFRELBos taurus-pH 4.0, 37°C708952-
0.079-AFPLEFIRELBos taurus-pH 4.0, 37°C708952-
0.18-AFPLEFKRELBos taurus-pH 4.0, 37°C708952-
0.01223-kappa-caseinBubalus bubalisQ9N1p5-698398-
0.02-kappa-caseinBos taurus-point mutant G343D36880-
0.066-kappa-caseinBos taurus--36883-
0.106-kappa-caseinHomo sapiens--36883-
0.89-kappa-caseinBos taurus--36878-
0.333-Leu-Ser-Phe(NO2)-Nle-Ala-Leu-O-methyl esterBos taurus-point mutant G243D36880 2D-image
1.11-Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OmeBos taurus-point mutant A115T36880 2D-image
0.85-Leu-Ser-Phe-Met-Ala-Ile-O-methyl esterBos taurus--36876 2D-image
0.016-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by D289M/Q298L mutant chymosin667593 2D-image
0.024-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by D289M/Q298L mutant chymosin667593 2D-image
0.028-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by Asp289Met mutant chymosin667593 2D-image
0.029-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by Gln298Leu mutant chymosin667593 2D-image
0.033-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by Gln298Leu mutant chymosin667593 2D-image
0.046-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by D289M/Q298L mutant chymosin667593 2D-image
0.054-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by Asp289Met mutant chymosin; hydrolysis of the Phe148 variant (cleavage L147-F148) by Asp289Met mutant chymosin667593 2D-image
0.059-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by wild type chymosin667593 2D-image
0.062-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by Gln298Leu mutant chymosin667593 2D-image
0.072-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by Asp289Met mutant chymosin667593 2D-image
0.083-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by wild type chymosin667593 2D-image
0.087-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by D289M/Q298L mutant chymosin667593 2D-image
0.095-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by Gln298Leu mutant chymosin667593 2D-image
0.105-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by wild type chymosin667593 2D-image
0.111-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by wild type chymosin667593 2D-image
0.065-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by Asp289Met mutant chymosin667593 2D-image
0.114-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by D289M/Q298L mutant chymosin667593 2D-image
0.229-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by Gln298Leu mutant chymosin667593 2D-image
0.25-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by D289M/Q298L mutant chymosin667593 2D-image
0.288-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by Asp289Met mutant chymosin667593 2D-image
0.304-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by wild type chymosin667593 2D-image
0.375-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by wild type chymosin667593 2D-image
0.463-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by Gln298Leu mutant chymosin667593 2D-image
0.34-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-O-methyl esterBos taurus--36876 2D-image
8.5-Ser-Phe-Met-Ala-Ile-O-methyl esterBos taurus--36876 2D-image
0.077-undecapeptide analogue to chymosin sensitive region of bovine kappa caseinCamelus dromedarius--667435-
0.165-undecapeptide analogue to chymosin sensitive region of bovine kappa caseinBos taurus--667435-
0.056-undecapeptide analogue to chymosin sensitive region of camel kappa caseinCamelus dromedarius--667435-
0.134-undecapeptide analogue to chymosin sensitive region of camel kappa caseinBos taurus--667435-
6.9-Leu-Ser-Phe-Met-Ala-O-methyl esterBos taurus--36876 2D-image
additional information-additional informationBos taurus-Km of kappa-casein related peptides36876-
additional information-additional informationBos taurus--36890-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.12-Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by recombinant chymosin667763 2D-image
0.16-Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by transgenic chymosin667763 2D-image
1.6-Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
1.4-Abz-A-A-F-F-A-A-p-nitroanilideBos taurus-hydrolysis by calf chymosin667763 2D-image
0.02-Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by transgenic chymosin667763 2D-image
0.11-Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by recombinant chymosin667763 2D-image
0.8-Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
0.27-Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
0.48-Abz-A-A-F-F-p-nitroanilideBos taurus-hydrolysis by calf chymosin667763 2D-image
0.06-Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by transgenic chymosin or recombinat chymosin667763 2D-image
0.14-Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamineBos taurus-hydrolysis by calf chymosin667763 2D-image
2600-AFPLEFERELBos taurus-pH 4.0, 37°C708952-
290-AFPLEFFRELBos taurus-pH 4.0, 37°C708952-
427-AFPLEFIRELBos taurus-pH 4.0, 37°C708952-
29-AFPLEFKRELBos taurus-pH 4.0, 37°C708952-
28NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by wild type chymosin667593 2D-image
12-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by Gln298Leu mutant chymosin667593 2D-image
16-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by D289M/Q298L mutant chymosin667593 2D-image
17-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by Gln298Leu mutant chymosin; hydrolysis of the Phe148 variant (cleavage F147-R148) by D289M/Q298L mutant chymosin667593 2D-image
22-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by D289M/Q298L mutant chymosin667593 2D-image
27-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by D289M/Q298L mutant chymosin667593 2D-image
30-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by Gln298Leu mutant chymosin667593 2D-image
32-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by Asp289Met mutant chymosin667593 2D-image
35-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by Asp289Met mutant chymosin667593 2D-image
39-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage L147-F148) by Asp289Met mutant chymosin667593 2D-image
41-NT/NMN 142-151Callithrix jacchus-hydrolysis of the parent peptide by wild type chymosin667593 2D-image
42-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by Asp289Met mutant chymosin667593 2D-image
46-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Glu148 variant by wild type chymosin667593 2D-image
49-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by Gln298Leu mutant chymosin667593 2D-image
191-NT/NMN 142-151Callithrix jacchus-hydrolysis of the Phe148 variant (cleavage F147-R148) by wild type chymosin667593 2D-image
12-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by D289M/Q298L mutant chymosin667593 2D-image
14-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by Asp289Met mutant chymosin667593 2D-image
43-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by D289M/Q298L mutant chymosin667593 2D-image
52-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by Gln298Leu mutant chymosin667593 2D-image
63-POm C165-174Callithrix jacchus-hydrolysis of the Glu171 variant by wild type chymosin667593 2D-image
90-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by Gln298Leu mutant chymosin667593 2D-image
101-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by Asp289Met mutant chymosin667593 2D-image
219-POm C165-174Callithrix jacchus-hydrolysis of the parent peptide by wild type chymosin667593 2D-image
11.7-undecapeptide analogue to chymosin sensitive region of bovine kappa caseinCamelus dromedarius--667435-
44.3-undecapeptide analogue to chymosin sensitive region of bovine kappa caseinBos taurus--667435-
4.3-undecapeptide analogue to chymosin sensitive region of camel kappa caseinBos taurus--667435-
5.1-undecapeptide analogue to chymosin sensitive region of camel kappa caseinCamelus dromedarius--667435-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
790-AFPLEFERELBos taurus-pH 4.0, 37°C7089520
7100-AFPLEFFRELBos taurus-pH 4.0, 37°C7089520
5400-AFPLEFIRELBos taurus-pH 4.0, 37°C7089520
160-AFPLEFKRELBos taurus-pH 4.0, 37°C7089520

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional information-Bos taurus--35015

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
2.5-Felis catus--36877
3.7-Bos taurus-isoform chymosin B708236
4-Bos taurus--35015
4-Callithrix jacchus--667593
4.2-Bos taurus-isoform chymosin A708236
4.5-Bubalus bubalisQ9N1p5recombinant chymosin698398
4.9-Bos taurus-for proteolysis of undecapeptide analogue to chymosin sensitive region of the bovine kappa casein667435
5-Bos taurus--36878
5.1-Camelus dromedarius-for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein667435
5.5-Capra hircusQ5VK60-686199

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
15Felis catus-acid-denatured hemoglobin, pH 1: about 80% of maximum activity, pH 5: about 30% of maximum activity36877
26Bos taurus--35015
26.7Bos taurus, Camelus dromedarius--667435
310Bos taurus-pH 3: about 80% of maximum activity, pH 10: about 20% of maximum activity36878
4.5-Bos taurus-using alpha- and beta-casein as substrate708236
4.65.6Bos taurus--669642
4.85-Camelus dromedarius-calculated isoelectric point667435
5.58Capra hircusQ5VK60sharp decline of activity up to pH 5.8, moderate decline at higher pH with complete loss of activity at pH 8686199
5.5-Camelus dromedarius-measured isoelectric point667435
5.5-Bos taurus-using kappa-casein as substrate708236
5.6-Bos taurus--669642
5.8-Bos taurus-using whole casein as substrate708236

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3050Bos taurus--708236
30-Bos taurus-assay at36875, 36880, 36882, 36891
30-Capra hircusQ5VK60milk clotting activity686199
37-Bos taurus--35015
37-Bubalus bubalisQ9N1p5-698398
42-Bos taurus, Camelus dromedarius-for proteolysis of the undecapeptide analogue to chymosin sensitive region of bovine kappa casein667435
47-Camelus dromedarius-for proteolysis of the undecapeptide analogue to chymosin sensitive region of camel kappa casein667435
50-Bos taurus--36878
55-Capra hircusQ5VK60proteolytic activity686199
56-Bos taurus-for proteolysis of the undecapeptide analogue to chymosin sensitive region of camel kappa casein667435
additional information-Capra hircusQ5VK60the substrate temperature was found to influence milk clotting activity, optimum substrate temperature is 65°C686199

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
552.5Bos taurus--667435
555Camelus dromedarius--667435
2060Bos taurus-20°C: about 25% of maximum activity, 60°C: about 50% of maximum activity36878
2545Bubalus bubalisQ9N1p5-698398
3060Capra hircusQ5VK60milk 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 activity686199
additional information-Capra hircusQ5VK60the 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°C686199

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4.55-Bos taurus-isoelectric focusing708236
4.6-Bos taurus-recombinant chymosin687952

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
abdomenCapra hircusQ5VK60enzyme extracted from abdomasal tissue of 15 days old kid686199Manually annotated by BRENDA team
abomasumBos taurus--35015, 36873, 667763Manually annotated by BRENDA team
abomasumCamelus dromedarius--667435Manually annotated by BRENDA team
abomasumBubalus bubalisQ9N1p5-698398Manually annotated by BRENDA team
commercial preparationBos taurus--708952Manually annotated by BRENDA team
epithelial cellCamelus dromedarius--667435Manually annotated by BRENDA team
gastric mucosaFelis catus--36877Manually annotated by BRENDA team
milkBos taurus-transgenic sheep milk667763Manually annotated by BRENDA team
milkBos taurus--668957Manually annotated by BRENDA team
mucosaCamelus dromedarius--667435Manually annotated by BRENDA team
stomachBos taurus--36872, 36882Manually annotated by BRENDA team
stomachSus scrofa--36888Manually annotated by BRENDA team
stomachCapra hircusQ5VK60produced in the fourth stomach of milk fed ruminants as inactive precursor prochymosin686199Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
additional informationBos taurus-rennet from abomasal tissue from a local indigenous breed-669642Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1cms, downloadSCOP (1cms)CATH (1cms)Bos taurus
1czi, downloadSCOP (1czi)CATH (1czi)Bos taurus
3cms, downloadSCOP (3cms)CATH (3cms)Bos taurus
4aa8, downloadSCOP (4aa8)CATH (4aa8)Bos taurus
4cms, downloadSCOP (4cms)CATH (4cms)Bos taurus
4aa9, downloadSCOP (4aa9)CATH (4aa9)Camelus dromedarius
2hb3, downloadSCOP (2hb3)CATH (2hb3)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
30700-Bos taurus-amino acid composition36882
33000-Bos taurus-gel filtration36882
35600-Camelus dromedarius-calculated peptide mass, SDS-PAGE667435
35600-Bos taurus-when the proenzyme is brought to pH 4.2, removal of 42 N-terminal residues results in an active form of chymosin of 35600 Da708236
36000-Bos taurus-purified chymosin, gel filtration669642
36300-Bos taurus-two-dimensional electrophoresis technique36872
36500-Bos taurus-sedimentation, diffusion36882
40000-Camelus dromedarius-apparent molecular weight, determined by comparison to a Novex Mark12TM667435
additional information-Bos taurus--36882

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Rhizomucor pusillus-x * 44000, SDS-PAGE650661
?Capra hircusQ5VK60x * 36000, SDS-PAGE686199
?Bubalus bubalisQ9N1p5x * 36000, SDS-PAGE, recombinant chymosin698398
additional informationBos taurus-? * 36000, SDS-PAGE35015
additional informationFelis catus-? * 36000, SDS-PAGE, similar enzyme36877

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
glycoproteinRhizomucor pusillus-12% glycosylated, oligomannoside attached covalently650661
additional informationBos taurus-insertion of a glycosylation site (S351T), glycosylation has significant inhibitory effect but this can be circumvented by deglycosylation with endoglucosidase H687865

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bos taurus-36871, 36882, 36894
loop exchange mutantBos taurus-36892
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 simulationsBos taurus-707523
point mutantsBos taurus-36880, 36891
prochymosin mutantBos taurus-36890

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
23.8Camelus dromedarius--667435
26Bos taurus-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 enzyme667763
26.5Bos taurus-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 7.0708236
2-Bos taurus--36882
3.5-Bos taurus-rapid loss of activity36882
5.36.3Bos taurus-highest stability36882
7-Bos taurus-rapid loss of activity above36882

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5-Bos taurus-very stable below, suspension of crystals36882
2550Bos taurus-transgenic chymosin loses activity slightly faster than abomasal enzyme and recombinant enzyme667763
25-Rhizomucor pusillus-most stable at pH 5.0, denaturation can be fitted to the two-state irreversible model650661
4055Camelus dromedarius-no residual clotting activities at temperatures higher than 55°C667435
45-Bos taurus-about 25% loss of activity after 60 min36874
5060Bos taurus-chymosin is stable up to 50°C and a relative milk-clotting activity of 50% is recorded when the temperature is raised to 60°C708236
50-Bos taurus-about 80% loss of activity after 30 min36874
55-Bos taurus-95% loss of activity after 10 min36874
55-Capra hircusQ5VK60stable up to 55°C, more thermostable than cattle chymosin and equally stable as buffalo chymosin686199
65-Rhizomucor pusillus-transition midpoint650661
additional information-Rhizomucor pusillus-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 endotherms650661

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
ureaBos taurus-chymosin loses 50% of its activity after incubation in 4.6 M urea at 37°C for 30 min708236

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, at pH 3.0 and 6.2, 3 days, maximum stabilityBos taurus-708236
very stable below 5°C, suspension of crystalsBos taurus-36882
-20°C, Tris-HCl buffer, pH 8.0, glycerolCallithrix jacchus-667593

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bos taurus-35015, 36882, 36890
by affinity chromatography on a bacitracin-Sepharose columnBos taurus-667763
DEAE-cellulose column chromatography, gel filtrationBos taurus-708236
extraction by application of ultrasoundBos taurus-36873
gel filtration and anion-exchange chromatographyBos taurus-669642
purification by partitioning between aqueous two-phase systemsBos taurus-687952
-Callithrix jacchus-667593
by affinity chromatography MIMO1300 matrixCamelus dromedarius-667435
resolves into three major peaks in DEAE chromatographyCapra hircusQ5VK60686199
similar enzymeFelis catus-36877
-Rhizomucor pusillus-650661
-Sus scrofa-36888

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bos taurus-36869, 36870, 36874
expressed as inclusion bodies in Escherichia coliBos taurus-687952
expressed in Escherichia coli and in Saccharomyces cerevisiaeBos taurus-708236
expression in Aspergillus nigerBos taurus-710493
expression in Kluyveromyces lactisBos taurus-667763
loop exchange mutant expressed in Trichoderma reeseiBos taurus-36892
point mutants expressed in Escherichia coli and Trichoderma reeseiBos taurus-36880, 36889
prochymosin fusion product expressed in Escherichia coliBos taurus-36890
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 TDNSTBos taurus-687865
-Bubalus bubalisQ9N1p5698398
expression in Saccharomyces cerevisiae strain INVSC1Callithrix jacchus-667593
expression in Aspergillus niger var. awamori dgr246pyrGCamelus dromedarius-667435
prochymosin cDNA, expressed as a NusA fusin protein in Escherichia coli, low level of milk clotting activity after activation at acidic pHCapra hircus-686839
expression in Pichia pastorisRhizomucor pusillus-650661

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
A115TBos taurus-reduction of Km compared to wild-type36880
D304ABos taurus-pH optima shift36893
D304A/T218ABos taurus-double mutant, substrate-specificity-pocket variant36889
D304A/T218ABos taurus--36891
G243DBos taurus-increase of Km compared to wild-type36880
G244DBos taurus-pH optima shift36893
Q288KBos taurus--36889
S351TBos taurus-insertion of a glycosylation site in the linker region between chymosin and glucoamylase, strongly improves enzyme secretion687865
T218ABos taurus-pH optima shift36889, 36891, 36893
D289M/Q298LCallithrix jacchus-decreased hydrolytic activity667593
additional informationCallithrix jacchus-Asp289Met mutant, Gln298Leu mutant, hydrolytic activity toward peptides having Lys at P'1 decreases significantly, mainly because of a decrease in the turnover values667593

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
-Bos taurus-36874
oxidative refolding of solubilized enzyme obtained from inclusion bodies at pH 2 to obtain autoconversion of prochymosin to active chymosinBos taurus-687952

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
food industryBos taurus-used for the production of dairy products687229, 687241
food industryBos taurus-coagulant for cheese making708236
food industryCapra hircusQ5VK60used as milk coagulant in cheese preparation686199
synthesisBos taurus-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 preparations710493
additional informationCamelus dromedarius-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 chymosin667435

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
AdenocarcinomaImmunocytochemical evidence for gastric proteases in adenocarcinoma of the stomach. PubMed
Alkalosis[A case of severe hypokalemia caused by a Chinese herbal remedy (Yokukansan) in an 81-year-old woman with dementia]. PubMed
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] PubMed
Anemia, PerniciousThe Glands of the Stomach in Relation to Pernicious Anaemia; with Special Reference to the Glands in the Pyloric Region: (Section of Medicine). PubMed
Corneal Neovascularization[Mechanisms and regulation of corneal neovascularization] PubMed
CystsTHE NEOPLASTIC POTENTIALITIES OF MOUSE EMBRYO TISSUES : III. THE TUMORS ELICITED FROM GASTRIC EPITHELIUM. PubMed
EnteritisContribution to some phenotypical characteristics of Vibrio cincinnatiensis. Studies in one strain of a diarrhoeic human patient and in two isolates from aborted bovine fetuses. PubMed
Fetal Growth Retardation[Compensatory hypertension and fetal heart remodeling: from adaptation to pathology] PubMed
Hyperaldosteronism[A case of severe hypokalemia during emergency surgery caused by long-term administration of Shakuyaku-kanzo-to]. PubMed
Hyperaldosteronism[A rare case of primary aldosteronism caused by bilateral functioning adrenocortical adenomas with renal cell carcinoma] PubMed
Hyperaldosteronism[The accuracy of combining aldosterone to renin ratio and low renin level in diagnosing primary aldosteronism] PubMed
HypertensionA case of primary aldosteronism caused by multiple adrenocortical macronodules. PubMed
HypertensionClinical laboratory in the biochemical evaluation of hypertension in Nigeria. PubMed
Hypertension[Blood rennin and hypertensinase in hypertension.] PubMed
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] PubMed
Hypertension[Retroperitoneal laparoscopic management of primary aldosteronism with report of 130 cases] PubMed
Hypertension[Subclinical endothelial inflammation markers in a family with type I familial hyperaldosteronism caused by a de novo mutation] PubMed
Hypertension, Pulmonary[Effects of continuous adenosine infusion on pulmonary hypertension in chronically hypoxic rats] PubMed
Hypertrophy, Left Ventricular[Heat shock proteins 70 kD as a new marker of lesions to target organs in hypertension] PubMed
Hypoaldosteronism[A case of severe hypokalemia caused by a Chinese herbal remedy (Yokukansan) in an 81-year-old woman with dementia]. PubMed
HypokalemiaA case of primary aldosteronism caused by multiple adrenocortical macronodules. PubMed
Hypokalemia[A case of severe hypokalemia caused by a Chinese herbal remedy (Yokukansan) in an 81-year-old woman with dementia]. PubMed
Hypokalemia[Retroperitoneal laparoscopic management of primary aldosteronism with report of 130 cases] PubMed
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] PubMed
HypothyroidismArterial hypertension and thyroid disorders: What is important to know in clinical practice? PubMed
InfectionMajor technological advances and trends in cheese. PubMed
Insulin Resistance[Effect of modified liberation doxazosin on blood pressure, insulin resistance, and catecholamine secretion in patients with true resistant hypertension] PubMed
Liver DiseasesStudy of substance P, renin and aldosterone in chronic liver disease in Egyptian children. PubMed
MeaslesAvoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies? PubMed
MumpsAvoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies? PubMed
NeoplasmsImmunocytochemical evidence for gastric proteases in adenocarcinoma of the stomach. PubMed
Neoplasms[A case of ruptured multiple cerebral aneurysms associated with primary aldosteronism] PubMed
Neoplasms[Reninoma: a rare but curable cause of high blood pressure, a case report] PubMed
ObesityThe impact of obesity on drug prescribing in primary care. PubMed
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] PubMed
Pre-EclampsiaThe relationship between aldosterone to renin ratio and RI value of the uterine artery in the preeclamptic patient vs. normal pregnancy. PubMed
Proteinuria[Chronic kidney disease: therapy and care]. PubMed
Pulmonary FibrosisRecent reports about enzymes related to the synthesis of prostaglandin (PG) F(2) (PGF(2?) and 9?, 11?-PGF(2)). PubMed
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] PubMed
RubellaAvoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies? PubMed
Sexually Transmitted DiseasesAvoidance of oxidative-stress perturbation in yeast bioprocesses by proteomic and genomic biostrategies? PubMed
Sleep Apnea, Obstructive[The changes of some vasoactive substances after operation in patients with obstructive sleep apnea-hypopnea syndrome] PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
30594Mabrouk, S.S.; Amr, A.S.; Abdel-Fattah, A.F.A rennin-like enzyme from Penicillium expansumAgric. Biol. Chem.40419-4201976Penicillium expansum-
35015Malak, 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 propertiesComp. Biochem. Physiol. B11357-621996Bos taurus PubMed
36869Moir, 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 chymosinGene19127-1381982Bos taurus PubMed
36870Beppu, T.The cloning and expression of chymosin (rennin) genes in microorganismsTrends Biotechnol.185-891983Bos taurus-
36871Gustchina, 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-caseinFEBS Lett.37960-621996Bos taurus PubMed
36872Kleinert, T.; Lange, I.; Roesicke, B.; Honig, A.; Schleusener, R.Characterization and preparation of chymosin from calf rennet samples by means of isoelectric focusingActa Biotechnol.8367-3751988Bos taurus-
36873Zayas, J.F.Properties and quality characteristics of rennin extracted by ultrasoundBiotechnol. Bioeng.29969-9751987Bos taurus PubMed
36874Kawaguchi, Y.; Kosugi, S.; Sasaki, K.; Uozumi, T.; Beppu, T.Production of chymosin in Escherichia coli cells and its enzymatic propertiesAgric. Biol. Chem.511871-18771987Bos taurus-
36875McCaman, M.T.; Andrews, W.H.; Files, J.G.Enzymatic properties and processing of bovine prochymosin synthezised in Escherichia coliJ. Biotechnol.2177-1901985Bos taurus-
36876Raap, 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 predictionArch. Biochem. Biophys.221117-1241983Bos taurus PubMed
36877Jensen, T.; Axelsen, N.H.; Foltmann, B.Isolation and partial characterization of prochymosin and chymosin from catBiochim. Biophys. Acta705249-2561982Felis catus PubMed
36878Miyoshi, M.; Yoon, C.H.; Ibuki, F.; Kanamori, M.The characterization of rennin action on kappa-casein using CM-celluloseAgric. Biol. Chem.40347-3521976Bos taurus-
36879Chang, W.J.; Takahashi, K.The structure and function of acid proteases. III. Isolation and characterization of the active-site peptides from bovine renninJ. Biochem.76467-4741974Bos taurus PubMed
36880Williams, M.G.; Wilsher, J.; Nugent, P.; Mills, A.; Dhanaraj, V.; Fabry, M.; Sedlacek, J.; Uusitalo, J.M.; Penttila, M.E.; Pitts, J.E.; Blundell, T.L.Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosinProtein Eng.10991-9971997Bos taurus PubMed
36881Akaeda, H.; Miura, H.; Mikami, M.Studies on the rennin inhibitor in serum Part II: Inhibiting action on rennin coagulation by alpha2-macroglobulinNippon Nogeikagaku Kaishi454491971Capra hircus, Equus caballus, Homo sapiens, Oryctolagus cuniculus, Ovis aries, Sus scrofa-
36882Foltmann, B.Prochymosin and chymosin (prorennin and rennin)Methods Enzymol.19421-4361970Bos taurus-
36883Azuma, 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 pepsinAgric. Biol. Chem.482025-20311984Bos taurus, Homo sapiens-
36884Abdel-Fattah, A.F.; Mabrouk, S.S.; El-Hawwary, N.M.Production and some properties of rennin-like milk-clotting enzyme from Penicillium citrinumJ. Gen. Microbiol.70151-1551972Penicillium citrinum-
36885Abdel-Fattah, A.F.; Abdel-Mohsen, S.I.; El-Aassar, S.A.Purification and properties of rennin-like enzyme from Absidia cylindrosporaZentralbl. Mikrobiol.14237-401987Absidia cylindrospora-
36886Abdel-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 enzymeZentralbl. Mikrobiol.14231-351987Absidia cylindrospora-
36888Houen, G.; Madsen, M.T.; Harlow, K.W.; Lonblad, P.; Foltmann, B.The primary structure and enzymic properties of porcine prochymosin and chymosinInt. J. Biochem. Cell Biol.28667-6751996Sus scrofa PubMed
36889Pitts, J.E.; Quinn, D.; Uusitalo, J.; Penttilae, M.Protein engineering of chymosin and expression in Trichoderma reeseiFood Biotechnol.19663-6661991Bos taurus PubMed
36890Strop, 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 chymosinBiochemistry299863-98711990Bos taurus PubMed
36891Pitts, 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 reeseiJ. Biotechnol.2869-831993Bos taurus PubMed
36892Nugent, 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 rhizopuspepsinProtein Eng.9885-8931996Bos taurus PubMed
36893Mantafounis, D.; Pitts, J.Protein engineering of chymosin; modification of the optimum pH of enzyme catalysisProtein Eng.3605-6091990Bos taurus PubMed
36894Gustchina, 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 reactionsAdv. Exp. Med. Biol.436179-1841998Bos taurus PubMed
650661Beldarrain, A.; Acosta, N.; Montesinos, R.; Mata, M.; Cremata, J.Characterization of Mucor pusillus rennin expressed in Pichia pastoris: enzymic, spectroscopic and calorimetric studiesBiotechnol. Appl. Biochem.3177-842000Rhizomucor pusillus-
667435Kappeler, 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 milkBiochem. Biophys. Res. Commun.342647-6542006Bos taurus, Camelus dromedarius PubMed
667593Kageyama, T.Role of S1 loop residues in the substrate specificities of pepsin A and chymosinBiochemistry4315122-151302004Callithrix jacchus PubMed
667763Starovoitova, 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 formsBiochemistry (Moscow)71320-3242006Bos taurus PubMed
668957Huppertz, 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 serumInt. dairy J.16691-6962006Bos taurus-
669642Moschopoulou, E.E.; Kandarakis, I.G.; Alichanidis, E.; Anifantakis, E.M.Purification and characterization of chymosin and pepsin from kidJ. Dairy Res.7349-572006Bos taurus PubMed
686199Kumar, 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.145108-1132006Capra hircus PubMed
686839Kumar, A.; Sharma, J.; Grover, S.; Mohanty, A.K.; Batish, V.K.Molecular cloning and expression of goat (Capra hircus) prochymosin in E. coliFood Biotechnol.2157-692007Capra hircus-
687104Molle, D.; Jean, K.; Guyomarch, F.Chymosin sensitivity of the heat-induced serum protein aggregates isolated from skim milkInt. Dairy J.161435-14412006Bos taurus-
687229Bansal, N.; Fox, P.F.; McSweeney, P.L.Aggregation of rennet-altered casein micelles at low temperaturesJ. Agric. Food Chem.553120-31262007Bos taurus PubMed
687241Renan, 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 aggregatesJ. Agric. Food Chem.556736-67452007Bos taurus PubMed
687865van den Brink, H.J.; Petersen, S.G.; Rahbek-Nielsen, H.; Hellmuth, K.; Harboe, M.Increased production of chymosin by glycosylationJ. Biotechnol.125304-3102006Bos taurus PubMed
687952Reh, G.; Spelzini, D.; Tubio, G.; Pico, G.; Farruggia, B.Partition features and renaturation enhancement of chymosin in aqueous two-phase systemsJ. Chromatogr. B86098-1052007Bos taurus PubMed
698398Vallejo, J.A.; Ageitos, J.M.; Poza, M.; Villa, T.G.Cloning and expression of buffalo active chymosin in Pichia pastorisJ. Agric. Food Chem.5610606-106102008Bubalus bubalis PubMed
707523Palmer, D.S.; Christensen, A.U.; Sörensen, J.; Celik, L.; Qvist, K.B.; Schiott, B.Bovine chymosin: a computational study of recognition and binding of bovine kappa-caseinBiochemistry492563-25732010Bos taurus PubMed
708213Hidalgo, M.E.; Pires, M.S.; Risso, P.H.A study on bovine kappa-casein aggregation after the enzymatic action of chymosinColloids Surf. B Biointerfaces76556-5632010Bos taurus PubMed
708236Kumar, A.; Grover, S.; Sharma, J.; Batish, V.K.Chymosin and other milk coagulants: sources and biotechnological interventionsCrit. Rev. Biotechnol.30243-2582010Bos taurus PubMed
708952Kageyama, H.; Ueda, H.; Tezuka, T.; Ogasawara, A.; Narita, Y.; Kageyama, T.; Ichinose, M.Differences in the P1' substrate specificities of pepsin A and chymosinJ. Biochem.147167-1742010Bos taurus PubMed
710493Justesen, 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 proteinProtein Sci.181023-10322009Bos taurus PubMed
717696Sorensen, 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-caseinJ. Agric. Food Chem.595636-56472011Bos taurus, Camelus dromedarius PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.4.23.4)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)