Information on EC 3.4.23.23 - Mucorpepsin

Word Map on EC 3.4.23.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.23.23
-
RECOMMENDED NAME
GeneOntology No.
Mucorpepsin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
-
CAS REGISTRY NUMBER
COMMENTARY hide
148465-73-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Mucor renninus
strain M-105
-
-
Manually annotated by BRENDA team
strain M-105
-
-
Manually annotated by BRENDA team
Penicillium duponti
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
azocasein + H2O
?
show the reaction diagram
Benzyloxycarbonyl-Gly-Phe-Phe + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Pro-L-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-L-Glu-L-Tyr + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-L-Phe-L-Leu + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-L-Phe-L-Tyr + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-L-Tyr-L-Leu + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Phe-Tyr + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
casein + H2O
fragments of casein
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
Hemoglobin + H2O
Hydrolyzed hemoglobin
show the reaction diagram
-
-
-
-
Kappa-casein + H2O
Hydrolyzed kappa-casein
show the reaction diagram
L-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
L-Leu-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
milk + H2O
?
show the reaction diagram
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized B-chain of insulin
show the reaction diagram
Peptides + H2O
Hydrolyzed peptides
show the reaction diagram
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
show the reaction diagram
Proteins + H2O
Hydrolyzed proteins
show the reaction diagram
soybean meal + H2O
?
show the reaction diagram
Val-Tyr-Val + H2O
?
show the reaction diagram
-
-
-
-
-
wheat bran + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
milk + H2O
?
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
2,4-Dinitro-1-fluorobenzene
-
-
CP-113972
-
i.e. (2R,3S)-isopropyl 3-[(L-prolyl-p-iodo-L-phenylalanyl-S-methyl-cysteinyl)amino-4]-2-hydroxybutanoate, human renin inhibitor
Diazo-H-tetrazole
-
-
Diazoacetyl-DL-norleucine methyl ester
Diazoacetyl-glycyl ethyl ester
-
in presence of copper ions
Iodine
Pepstatin
pepstatin A
Tetranitromethane
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.1
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5 - 16
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5
Penicillium duponti
-
-
3 - 3.5
3 - 3.5
-
-
3.5
Mucor renninus
-
-
3.5 - 3.6
-
acid protease D
3.7 - 3.8
-
acid protease C
additional information
Mucor renninus
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
more than 80% activity between pH 3.0 and pH 6.0
additional information
Mucor renninus
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
for milk-clotting activity
35
-
for proteolytic activity
40
-
acid protease D
49 - 55
-
Mucor pusillus
63
-
above, Mucor miehei
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.1
-
isoelectric focusing
4.2
-
isoelectric focusing
4.21
-
isoelectric focusing
5.1
Mucor renninus
-
isoelectric focusing
5.2
-
isoelectric focusing
5.5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
-
x * 16000
29000 - 32500
-
Mucor pusillus, gel filtration, sedimentation and diffusion data
33500
-
1 * 33500, SDS-PAGE
34000
-
x * 34000
38000
-
Mucor miehei
38700
-
gel filtration
41000
Penicillium duponti
-
x * 41000
41800
-
Mucor miehei, amino acid analysis
42000
-
Mucor miehei, SDS-PAGE
44000
-
SDS-PAGE
47000
-
x * 47000
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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
-
mutant Y75N in complex with human renin inhibitor CP-113972
-
structure and refinement at 2.0 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
-
acid protease C, highest stability at pH 4.0
30649
4 - 4.2
-
highest thermal stability
30659
4 - 8
-
acid protease D, highest stability at pH 5.0
30649
5
-
60°C, 10 min, highest stability
30668
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38
-
pH 3.0-6.0, 8 days, more than 90% of activity retained
40 - 60
-
stable up to 40°C, 26% residual proteolytic activity at 50°C, 13% residual proteolytic activity at 60°C
40
-
stable up to, acid protease D
45
-
stable up to, acid protease C
65
-
15 min, 40% loss of activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Urea, pH 6.0, 11 h stable
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation, mediated by methylene blue, inactivates
-
30650, 30668, 30672, 30678
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification by direct extraction of a fermentation system
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aspartic proteinase gene expressed in Pichia pastoris
-
in Escherichia coli
-
Mucor pusillus gene expressed in Saccharomyces cerevisiae
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y75N
-
crystallization data
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition