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Information on EC 3.4.23.23 - Mucorpepsin
for references in articles please use BRENDA:EC3.4.23.23
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.23 Aspartic endopeptidases
3.4.23.23 Mucorpepsin
IUBMB Comments
Isolated from the zygomycete fungi Mucor pusillus and M. miehei. The two species variants show 83% sequence identity and are immunologically crossreactive. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6
The enzyme appears in viruses and cellular organisms
- 3.4.23.23
- plasminogen
- plasmin
- fibrinogen
- clot
-
thrombolytic
- coagulation
-
fibrinolysis
- thrombosis
- proteinases
- urokinase
- venom
- pmsf
- pepstatin
- thrombus
-
snake
-
tissue-type
-
zymography
- nattokinase
- agkistrodon
- earthworm
- streptokinase
- natto
-
aprotinine
- rubellus
- contortrix
-
euglobulin
- copperhead
-
milk-clotting
-
direct-acting
-
amidolytic
- endothiapepsin
-
lumbricus
- rhizopuspepsin
-
gamma-chains
- eisenia
-
fibrinogenolytic
- fetida
-
plasminogen-free
- lebetina
-
vipera
- nutrition
Reaction Schemes
showHydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen
Synonyms
fibrinolytic enzyme, aspartyl proteinase, mucor rennin, mucor pusillus pepsin, mucor pusillus rennin, mucorpepsin, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid proteinase
aspartic protease
Aspartic proteinase
aspartyl proteinase
EC 3.4.23.6
-
-
formerly
-
EC 3.4.4.17
-
-
formerly, part transferred
-
fibrinolytic enzyme
Fromase 100
-
-
-
-
Fromase 46TL
-
-
-
-
MCAP
Mucor acid protease
-
-
-
-
Mucor acid proteinase
-
-
-
-
Mucor aspartic proteinase
-
-
-
-
Mucor miehei aspartic protease
-
-
-
-
Mucor miehei aspartic proteinase
-
-
-
-
Mucor pusillus emporase
-
-
-
-
Mucor rennin
Proteinase, Mucor aspartic
-
-
-
-
Mucor rennin
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins, favouring hydrophobic residues at P1 and P1'. Clots milk. Does not accept Lys at P1, and hence does not activate trypsinogen
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
148465-73-0
-
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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
2-aminobenzoyl-KLRMSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + MSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRSKKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SKKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRSSMQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SSMQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRSWKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + SWKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-KLRWSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-KLR + WSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-LSFMAIQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine + H2O
2-aminobenzoyl-LSF + MAIQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
Substrates: substrate derived from peptide sequence of kappa-casein
Products: -
Products: -
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized B-chain of insulin
-
Substrates: hydrolysis at: Phe1-Val2, Ala14-Leu15, Leu15-Tyr16, Tyr16-Leu17, Phe24-Phe25, Phe25-Tyr26, Tyr26-Thr27
Products: -
Products: -
?
Kappa-casein + H2O
Hydrolyzed kappa-casein
-
Substrates: -
Products: -
Products: -
?
Kappa-casein + H2O
Hydrolyzed kappa-casein
-
Substrates: -
Products: -
Products: -
?
Kappa-casein + H2O
Hydrolyzed kappa-casein
-
Substrates: -
Products: para-casein + glycopeptide, release of sialic acid from kappa-casein
Products: para-casein + glycopeptide, release of sialic acid from kappa-casein
?
milk + H2O
?
-
Substrates: high milk-clotting activity
Products: -
Products: -
?
N,N-dimethyl-casein + H2O
L-tyrosine + ?
Substrates: -
Products: -
Products: -
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
?
-
Substrates: -
Products: -
Products: -
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
?
Mucor subtilissimus UCP 1262
-
Substrates: -
Products: -
Products: -
?
Peptides + H2O
Hydrolyzed peptides
-
Substrates: -
Products: -
Products: -
?
Peptides + H2O
Hydrolyzed peptides
-
Substrates: carbobenzoxy-Phe-Met methyl ester containing the bond involved in milk clotting mechanism is not hydrolyzed unless it becomes part of a polypeptide with tails of carbobenzoxy-Phe-Met anchored on a polylysine chain
Products: -
Products: -
?
Peptides + H2O
Hydrolyzed peptides
-
Substrates: -
Products: -
Products: -
?
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
-
Substrates: -
Products: -
Products: -
?
Proteins + H2O
Hydrolyzed proteins
-
Substrates: preferentially hydrolyzes peptide bonds having an aromatic amino acid as carboxyl donor
Products: -
Products: -
?
Proteins + H2O
Hydrolyzed proteins
-
Substrates: involving aromatic residues
Products: -
Products: -
?
Proteins + H2O
Hydrolyzed proteins
-
Substrates: involving aromatic residues
Products: -
Products: -
?
succinyl-L-Ala-Ala-Pro-L-Phe-4-nitroanilide + H2O
?
-
Substrates: selective substrate
Products: -
Products: -
?
succinyl-L-Ala-Ala-Pro-L-Phe-4-nitroanilide + H2O
?
Mucor subtilissimus UCP 1262
-
Substrates: selective substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity against aromatic bulky or hydrophobic amino acid residues at both sides of the splitting point
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity against aromatic bulky or hydrophobic amino acid residues at both sides of the splitting point
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity against aromatic bulky or hydrophobic amino acid residues at both sides of the splitting point
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity against aromatic bulky or hydrophobic amino acid residues at both sides of the splitting point
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity against aromatic bulky or hydrophobic amino acid residues at both sides of the splitting point
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activation of trypsinogen
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows a preference for aromatic, basic, and nonpolar amino acids, particularly methionine, with specific cleavage of the peptide bond between phenylalanine and methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is cleaved autocatalytically into 2 major glycopeptides under alkaline conditions
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: milk clotting activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity against aromatic bulky or hydrophobic amino acid residues at both sides of the splitting point
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
milk + H2O
?
-
Substrates: high milk-clotting activity
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CP-113972
-
i.e. (2R,3S)-isopropyl 3-[(L-prolyl-p-iodo-L-phenylalanyl-S-methyl-cysteinyl)amino-4]-2-hydroxybutanoate, human renin inhibitor
Diazoacetyl-DL-norleucine methyl ester
-
if added with 78fold molar excess of Cu2+
Iodine
-
complete inhibition at pH 6.7, little loss of activity at pH 3.0-5.0
additional information
-
no effect with PMSF, p-chloromercuriphenylsulfonic acid or EDTA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0004
2-aminobenzoyl-KLRMSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.00085
2-aminobenzoyl-KLRSKKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.0005
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.000045
2-aminobenzoyl-KLRSSMQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.00011
2-aminobenzoyl-KLRSWKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.00015
2-aminobenzoyl-KLRWSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.000036
2-aminobenzoyl-LSFMAIQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
2-aminobenzoyl-KLRMSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
1.1
2-aminobenzoyl-KLRSKKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.35
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.045
2-aminobenzoyl-KLRSSMQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.12
2-aminobenzoyl-KLRSWKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
0.15
2-aminobenzoyl-KLRWSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1250
2-aminobenzoyl-KLRMSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
1294
2-aminobenzoyl-KLRSKKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
700
2-aminobenzoyl-KLRSSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
1000
2-aminobenzoyl-KLRSSMQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
1091
2-aminobenzoyl-KLRSWKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
1000
2-aminobenzoyl-KLRWSKQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
4722
2-aminobenzoyl-LSFMAIQ-N1-(2,4-dinitrophenyl)ethane-1,2-diamine
-
pH 6.5, 45°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 3.5
3.8
4.5
4.7
5.5
5.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
-
about 85% activity at pH 5.0, 100% activity at pH 5.5, about 90% activity at pH 6.0, about 65% activity at pH 6.5, about 40% activity at pH 7.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
50
55
60
60
-
purified mutant G186D/E13D and non-mutant enzymes act optimally at 60°C and later, they start losing their activity rapidly leading to complete inactivation at 75°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Mucor renninus
-
30566, 30589, 30641, 30642, 30643, 30645, 30646, 30652, 30655, 30656, 30659, 30660, 30661, 30664, 30665, 30667, 30669, 30673, 30674, 649247, 649270, 652776, 717133, 743030
-
-
brenda
-
30568, 30589, 30649, 30650, 30652, 30654, 30655, 30658, 30663, 30666, 30668, 30670, 30671, 30672, 30675, 30676, 30677, 30678, 30679, 30681, 30682, 650661, 667045, 717133, 754970, 755331
-
-
brenda
zygomycete fungus, previously called Mucor pusillus, strains IFO4578 and F27
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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.
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). A0A068RL61_9FUNG
518
0
54520
TrEMBL
-
A0A068RM05_9FUNG
501
0
52485
TrEMBL
other Location (Reliability: 2)
A0A068RFJ6_9FUNG
410
0
45486
TrEMBL
-
A0A068RT80_9FUNG
430
0
47339
TrEMBL
-
A0A068RNA1_9FUNG
537
0
56305
TrEMBL
-
A0A068RR92_9FUNG
431
0
46880
TrEMBL
-
A0A068S5G5_9FUNG
571
0
61974
TrEMBL
-
A0A068S4K5_9FUNG
495
0
53605
TrEMBL
-
A0A068SA06_9FUNG
384
0
42130
TrEMBL
-
A0A077WFS2_9FUNG
428
0
46668
TrEMBL
other Location (Reliability: 2)
A0A8H7VCG6_9FUNG
514
0
54454
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H7VLP8_9FUNG
463
0
49912
TrEMBL
Secretory Pathway (Reliability: 2)
A0AAD5K767_9FUNG
468
0
49927
TrEMBL
Secretory Pathway (Reliability: 1)
A0AAD5K0M2_9FUNG
455
0
50863
TrEMBL
Secretory Pathway (Reliability: 2)
A0AAD5KBG3_9FUNG
483
0
52481
TrEMBL
Secretory Pathway (Reliability: 3)
A0AAD5KRN0_9FUNG
466
0
49842
TrEMBL
Secretory Pathway (Reliability: 1)
A0AAD5PDR1_9FUNG
391
0
42393
TrEMBL
Secretory Pathway (Reliability: 2)
A0AAD7V5M3_9FUNG
495
0
53577
TrEMBL
Secretory Pathway (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000 - 32500
-
Mucor pusillus, gel filtration, sedimentation and diffusion data
33000
35000
38500
additional information
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
-
Mucor pusillus, a single polypeptide chain containing 361 amino acid residues, cross-linked by two disulfide bonds, amino acid sequence analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
6% covalently bound carbohydrate (hexosamine and neutral hexoses)
glycoprotein
-
Mucor miehei: D-mannose, D-glucose, D-galactose, N-acetyl-D-glucosamine in the ratio 7:2:1:2
glycoprotein
-
a sugar moiety composed of 2 GlcNAc residues and four neutral sugar residues are asparagine-linked to the chain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallizes in the orthorhombic space group P2(1)2(1)2(1), a : 41.86 A, b : 51.21 A, c : 174.24 A
-
hanging-drop method, orthorhombic space group P2(1)2(1)2(1), cell dimensions a : 41.86 A, b : 51.21 A, c : 174.24 A
-
small thin needle-like seed crystals of the native enzyme grown by the hanging-drop vapour-diffusion method, unit-cell dimensions a : 41.82 A, 51.21 A, c : 174.24 A, in complex with inhibitor pepstatin A, orthorhombic space group P2(1)2(1)2(1), isomorphous to native RMP crystals, unit-cell dimensions are a : 41.52 A, b : 50.82 A, c : 172.71 A
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N331Q
A101T
-
the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme
A101T/G186D
-
the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme
E13A
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
E13D
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
E13P
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
E13Q
-
the proteolytic activity of the mutant decreases remarkably to almost a half of that of non-mutant enzyme
G186D
-
the proteolytic activity of the mutant is similar to the non-mutant enzyme. The milk clotting activity of the mutant is increased compared to the non-mutant enzyme
G186D/E13D
-
the mutant shows a significant milk-clotting activity. The mutant rennet can decrease hydrolysis of protein during ripening of cheese. The mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity
G186D/E13Q
L287G
-
the mutant shows an increase in the ratio of clotting activity to proteolytic activity as compared to the wild type enzyme
T218A/T218S/L287G
-
the mutations lead to a significant decrease in proteolytic activity compared to the wild type enzyme
T218S
-
the mutation causes a low thermostability and moderate increase in the clotting activity compared to the wild type enzyme. The mutant shows a 3.34fold increase in the ratio of clotting activity to proteolytic activity as compared to the wild type enzyme. The mutant can serve as a promising milk coagulant that contributes to an optimal flavor development in mature cheese
G186D/E13Q
-
the mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity
G186D/E13Q
-
the mutant shows a significant milk-clotting activity. The mutant rennet can decrease hydrolysis of protein during ripening of cheese. The mutant has a reduction in thermostability along with a sharp decrease in proteolytic activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
3.3 - 3.8
the enzyme remains stable after 1 h at pH 3.3-3.6. The activity drops to about 60% and about 50% after 1 h at pH 3.7 and 3.8, respectively
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
at 37°C, the enzyme residual activity is 94 and 68% of the initial one after 120 and 150 min of incubation, respectively
40 - 60
-
stable up to 40°C, 26% residual proteolytic activity at 50°C, 13% residual proteolytic activity at 60°C
45
50 - 55
upon 60 min incubation period enzyme activity begins to decrease at a temperature above of 50 °C. After 1 h of incubation at 55°C, 75% of the unpurified enzyme's activity is retained
55
additional information
55
-
the wild type enzyme retains 88.6% activity after 60 min at 55°C. Mutant enzyme G186D/E13D loses 30% of its activity after 50 min at 55°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation, mediated by methylene blue, inactivates
-
30650, 30668, 30672, 30678
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-52 column chromatography and Sephadex G-100 gel filtration
-
partially purified by 30% (w/v) polyethylene glycol/ 13.2% (w/v) sodium sulfate aqueous two-phase systems
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
nutrition
-
wide industrial appplication as calf rennet substitutes in cheese manufacture
nutrition
-
used as a substitute for calf chymosin, making use of its milk-clotting activity
nutrition
-
Mucor rennin can be used as a substituting enzyme for calf chymosin in the cheese industry
nutrition
-
wide industrial appplication as calf rennet substitutes in cheese manufacture
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morihara, K.; Oka, T.
Comparative specificity of microbial acid proteinases for synthetic peptides. 3. Relationship with their trypsinogen activating ability
Arch. Biochem. Biophys.
157
561-572
1973
Rhizomucor miehei
brenda
Takahashi, K.; Chang, W.J.
The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin
J. Biochem.
80
497-506
1976
Rhizomucor pusillus
brenda
Dunn, B.M.; Jimenez, M.; Parten, B.F.; Valler, M.J.; Rolph, C.E.; Kay, J.
A systematic series of synthetic chromophoric substrates for aspartic proteinases
Biochem. J.
237
899-906
1986
Rhizomucor miehei, Rhizomucor pusillus
brenda
Rickert, W.S.; Elliott, J.R.
Acid proteases from species of Mucor: molecular weight on Mucor miehei protease from amino acid analysis data
Can. J. Biochem.
51
1638-1646
1973
Rhizomucor miehei
brenda
Ottesen, M.; Rickert, W.
The isolation and partial characterization of an acid protease produced by Mucor miehei
C. R. Trav. Lab. Carlsberg
37
301-325
1970
Rhizomucor miehei
brenda
Drohse, H.B.; Foltmann, B.
Specificity of milk-clotting enzymes towards bovine kappa-casein
Biochim. Biophys. Acta
995
221-224
1989
Rhizomucor miehei
brenda
Yamashita, T.; Tonouchi, N.; Uozomi, T.; Beppu, T.
Secretion of Mucor rennin, a fungal aspartic protease of Mucor pusillus, by recombinant yeast cells
Mol. Gen. Genet.
210
462-467
1987
Rhizomucor pusillus
brenda
Murata, K.; Kusakabe, I.; Kobayashi, H.; Akaike, M.; Park, Y.W.; Murakami, K.
Studies on the coagulation of soy milk protein by commercial proteinases
Agric. Biol. Chem.
51
385-389
1987
Rhizomucor miehei
-
brenda
Gray, G.L.; Hayenga, K.; Cullen, D.; Wilson, L.J.; Norton, S.
Primary structure of Mucor miehei aspartyl protease: evidence for a zymogen intermediate
Gene
48
41-53
1986
Rhizomucor miehei
brenda
Tonouchi, N.; Shoun, H.; Uozumi, T.; Beppu, T.
Cloning and sequencing of a gene for Mucor rennin, an aspartate protease from Mucor pusillus
Nucleic Acids Res.
14
7557-7568
1986
Rhizomucor pusillus
brenda
Khan, M.R.; Blain, J.A.; Patterson, J.D.E.
Partial purification of Mucor pusillus intracellular proteases
Appl. Environ. Microbiol.
45
94-96
1983
Rhizomucor pusillus
brenda
Ethoh, Y.; Shoun, H.; Arima, K.; Beppu, T.
Photo-oxidation of a histidyl residue of milk-clotting acid protease, Mucor rennin
J. Biochem.
91
747-753
1982
Rhizomucor pusillus
brenda
Fraile, E.R.; Muse, J.O.; Bernadinelli, S.E.
Milk-clotting enzyme from Mucor bacilliformis
Eur. J. Appl. Microbiol. Biotechnol.
13
191-193
1981
Mucor bacilliformis
-
brenda
Martin, P.; Raymond, M.N.; Bricas, E.; Dumas, B.R.
Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteases and chymosins A and B on a synthetic chromophoric hexapeptide
Biochim. Biophys. Acta
612
410-420
1980
Rhizomucor miehei, Rhizomucor pusillus
brenda
Belyauskaite, I.P.; Palubinskas, V.J.; Achenko, O.E.; Vesa, V.S.; Glemzha, A.A.
Purification and some properties of the extracellular acid proteases from Mucor renninus
Enzyme Microb. Technol.
2
37-44
1980
Mucor renninus
-
brenda
Khan, M.R.; Blain, J.A.; Patterson, J.D.E.
Extracellular proteases of Mucor pusillus
Appl. Environ. Microbiol.
37
719-724
1979
Rhizomucor pusillus
brenda
Etoh, Y.; Shoun, H.; Beppu, T.; Arima, K.
Milk-clotting enzyme from microorganisms. Part XII. Physicochemical and immunochemical studies on similarities of the acid proteases Mucor pusillus rennin and Mucor miehei rennin
Agric. Biol. Chem.
43
209-215
1979
Rhizomucor miehei, Rhizomucor pusillus
-
brenda
Rickert, W.S.; McBride-Warren, P.A.
Structural and functional determinants of Mucor miehei protease VI. Inactivation of the enzyme by diazoacetyl norleucine methyl esters, pepstatin and 1,2-epoxy-30(p-nitro-phenyoxy)propane
Biochim. Biophys. Acta
480
262-274
1977
Rhizomucor miehei
brenda
Takahshi, K.; Chang, W.J.; Arima, K.
The structure and function of acid proteases. IV. Inactivation of the acid protease from Mucor pusillus by acid protease-specific inhibitors
J. Biochem.
80
61-67
1976
Rhizomucor pusillus
brenda
Ledward, D.A.; Finch, A.; Rickert, W.S.
Structural and functional determinants of Mucor miehei protease. V. Enthalpy changes upon thermal denaturation in solution of varying pH
Biochim. Biophys. Acta
379
426-430
1975
Rhizomucor miehei
brenda
Rickert, W.S.; McBride-Warren, P.A.
Structural and functional determinants of Mucor miehei protease. IV. Nitration and spectrophotometric titration of tyrosine residues
Biochim. Biophys. Acta
371
368-378
1974
Rhizomucor miehei
brenda
Rickert, W.S.; McBride-Warren, P.A.
Structural and functional determinants of Mucor miehei protease. III. Isolation and composition of the carbohydrate moiety
Biochim. Biophys. Acta
336
437-444
1974
Rhizomucor miehei
-
brenda
Oka, T.; Ishino, K.; Tsuzuki, H.; Morihara, K.; Arima, K.
Specificity of a Renninlike enzyme from Mucor pusillus
Agric. Biol. Chem.
37
1177-1184
1973
Rhizomucor pusillus
-
brenda
Oka, T.; Morihara, K.
Comparative specificity of microbial acid proteinases for synthetic peptides. II. Effect of secondary interaction
Arch. Biochem. Biophys.
156
552-559
1973
Rhizomucor miehei
brenda
Oka, T.; Morihara, K.
Comparative specificity of microbial acid proteinases for synthetic peptides. I. Primary specificity
Arch. Biochem. Biophys.
156
543-551
1973
Rhizomucor miehei
brenda
Sanner, T.; Kovacs-Proszt, G.
Kinetic studies on the aggregation of kappa-casein by Mucor pusillus protease
Biochim. Biophys. Acta
303
68-76
1973
Rhizomucor pusillus
brenda
Sternberg, M.
Bond specificity, active site and milk clotting mechanism of the Mucor miehei protease
Biochim. Biophys. Acta
285
383-392
1972
Rhizomucor miehei
brenda
Arima, K.; Yu, J.; Iwasaki, S.
Milk-clotting enzyme for Mucor pusillus var Lindt
Methods Enzymol.
19
446-459
1970
Rhizomucor pusillus
-
brenda
Rickert, W.S.
Structural and functional determinants of Mucor miehei protease. I. Modification of the NH 2 terminus and lysine residues by carbamylation
Biochim. Biophys. Acta
271
93-101
1972
Rhizomucor miehei
brenda
Takahshi, K.; Mizobe, F.; Chang, W.J.
Inactivation of acid proteases from Rhizopus chinensis, Aspergillus saitoi and Mucor pusillus, and calf rennin by diazoactylnorleucine methyl ester
J. Biochem.
71
161-164
1972
Rhizomucor pusillus
brenda
Yu, J.; Tamura, G.; Arima, K.
Milk-clotting enzyme from microorganisms. IX. Reaction of diazo-1-H-tetrazole on mucor-rennin (crystalline milk-clotting enzyme)
Agric. Biol. Chem.
35
1398-1401
1971
Rhizomucor pusillus
-
brenda
Yu, J.; Tamura, G.; Arima, K.
Milk-clotting enzyme from microorganisms. VIII. Active center of milk-clotting enzyme (mucor-rennin) isolated from Mucor pusillus
Agric. Biol. Chem.
35
1194-1199
1971
Rhizomucor pusillus
-
brenda
Ottesen, M.; Rickert, W.
Acid protease of Mucor miehei
Methods Enzymol.
19
459-460
1970
Rhizomucor miehei
-
brenda
Voynick, I.M.; Fruton, J.S.
The comparative specificity of acid proteinases
Proc. Natl. Acad. Sci. USA
68
257-259
1971
Rhizomucor miehei
brenda
Arima, K.; Yu, J.; Iwasaki, S.; Tamura, G.
Milk-clotting enzyme from microorganisms. V. Purification and crystallization of Mucor rennin from Mucor pusillus var Lindt
Appl. Microbiol.
16
1727-1733
1968
Rhizomucor pusillus
brenda
Yu, J.; Tamura, G.; Arima, K.
Milk-clotting enzyme from microorganisms. VI. Properties of crystalline milk-clotting enzyme (Mucor rennin) isolated from Mucor pusillus var. Lindt
Biochim. Biophys. Acta
171
138-144
1969
Rhizomucor pusillus
brenda
Yu, J.; Liu, W.H.; Tamura, G.; Arima, K.
Release of sialic acid from kappa casein by mucor-rennin (milk-clotting enzyme) of Mucor pusillus
Agric. Biol. Chem.
32
1482-1483
1968
Rhizomucor pusillus
-
brenda
Yu, J.; Tamura, G.; Arima, K.
The active site of Mucor-rennin and reaction of calcium ion on milk coagulation
Agric. Biol. Chem.
32
1048-1050
1968
Rhizomucor pusillus
-
brenda
Somkuti, G.A.; Babel, F.J.
Purification and properties of Mucor pusillus acid protease
J. Bacteriol.
95
1407-1414
1968
Rhizomucor pusillus
brenda
Fernandez Lahore, H.M.; Miranda, M.V.; Fraile, E.R.; Biscoglio de Jimenez Bonino, M.J.; Cascone, O.
Partition behavior and purification of a Mucor bacilliformis acid protease in aqueous two-phase systems
Process Biochem.
30
615-621
1995
Mucor bacilliformis
-
brenda
Baudys, M.; Foundling, S.; Pavlik, M.; Blundell, T.; Kostka, V.
Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment
FEBS Lett.
235
271-274
1988
Rhizomucor pusillus
brenda
Newman, M.; Watson, F.; Roychowdhury, P.; Jones, H.; Badasso, M.; Cleasby, A.; Wood, S.P.; Ticke, I.J.; Blundell, T.L.
X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor pusillus
J. Mol. Biol.
230
260-283
1993
Rhizomucor pusillus
brenda
Yang, J.; Quail, J.W.
Structure of the Rhizomucor miehei aspartic proteinase complexed with the inhibitor pepstatin A at 2.7 ANG resolution
Acta Crystallogr. Sect. D
D55
625-630
1999
Rhizomucor miehei
-
brenda
Quail, J.W.; Yang, J.; Schneider, P.; Jia, Z.
Crystal structure of the Rhizomucor miehei aspartic proteinase
Adv. Exp. Med. Biol.
436
283-292
1998
Rhizomucor miehei
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
-
brenda
Yang, J.; Teplyakov, A.; Quail, J.W.
Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 ANG resolution
J. Mol. Biol.
268
449-459
1997
Rhizomucor miehei
brenda
Fernandez-Lahore, H.M.; Auday, R.M.; Fraile, E.R.; Biscoglio de Jimenez Bonino, M.; Pirpignani, L.; Machalinski, C.; Cascone, O.
Purification and characterization of an acid proteinase from mesophilic Mucor sp. solid-state cultures
J. Pept. Res.
53
599-605
1999
Mucor sp., Mucor sp. M-105
brenda
Murakami, K.; Takeuchi, K.; Beppu, T.; Horinouchi, S.
Structure of asparagine-linked oligosaccharides of an aspartic proteinase from the zygomycete fungus Rhizomucor pusillus
Microbiology
144
1369-1374
1998
Rhizomucor pusillus
-
brenda
Badasso, M.O.; Dhanaraj, V.; Wood, S.P.; Cooper, J.B.; Blundell, T.L.
Crystallization and X-ray analysis of the Y75N mutant of Mucor pusillus pepsin complexed with inhibitor
Acta Crystallogr. Sect. D
60
770-772
2004
Rhizomucor pusillus
brenda
Yegin, S.; Fernndez-Lahore, M.; Guvenc, U.; Goksungur, Y.
Production of extracellular aspartic protease in submerged fermentation with Mucor mucedo DSM 809
Afr. J. Biotechnol.
9
6380-6386
2010
Mucor mucedo, Mucor mucedo DSM 809
-
brenda
Yegin, S.; Fernandez-Lahore, M.; Jose Gama Salgado, A.; Guvenc, U.; Goksungur, Y.; Tari, C.
Aspartic proteinases from Mucor spp. in cheese manufacturing
Appl. Microbiol. Biotechnol.
89
949-960
2011
Mucor circinelloides, Rhizopus arrhizus, Aspergillus oryzae, Cryphonectria parasitica, Penicillium duponti, Rhizomucor pusillus, Rhizomucor miehei, Mucor hiemalis, Mucor renninus, Mucor racemosus f. racemosus, Amylomyces rouxii, Mucor bacilliformis
brenda
da Silva, R.R.; Souto, T.B.; de Oliveira, T.B.; de Oliveira, L.C.; Karcher, D.; Juliano, M.A.; Juliano, L.; de Oliveira, A.H.; Rodrigues, A.; Rosa, J.C.; Cabral, H.
Evaluation of the catalytic specificity, biochemical properties, and milk clotting abilities of an aspartic peptidase from Rhizomucor miehei
J. Ind. Microbiol. Biotechnol.
43
1059-1069
2016
Rhizomucor miehei
brenda
Kangwa, M.; Salgado, J.A.G.; Fernandez-Lahore, H.M.
Identification and characterization of N-glycosylation site on a Mucor circinelloides aspartic protease expressed in Pichia pastoris effect on secretion, activity and thermo-stability
AMB Express
8
157
2018
Mucor circinelloides (U5HT00), Mucor circinelloides DSM 2183 (U5HT00)
brenda
Nascimento, T.; Sales, A.; Porto, C.; Brandao, R.; de Campos-Takaki, G.; Teixeira, J.; Porto, T.; Porto, A.; Converti, A.
Purification of a fibrinolytic protease from Mucor subtilissimus UCP 1262 by aqueous two-phase systems (PEG/sulfate)
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
1025
16-24
2016
Mucor subtilissimus, Mucor subtilissimus UCP 1262
brenda
Yuqiu, L.; Tanhu, T.; Da, L.; Zhoulin, L.; Yanping, C.; Yuanyuan, J.; Xiangying, L.; Jinghui, W.; Qiyun, L.
Screening and characterization of a mutant fungal aspartic proteinase from Mucor pusillus
Open Biotechnol. J.
9
119-126
2015
Rhizomucor pusillus
-
brenda
Zhang, J.; Sun, Y.; Li, Z.; Luo, Q.; Li, T.; Wang, T.
Structure-based design of Mucor pusillus pepsin for the improved ratio of clotting activity/proteolytic activity in cheese manufacture
Protein Pept. Lett.
22
660-667
2015
Rhizomucor pusillus
-
brenda
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