Information on EC 3.4.23.40 - Phytepsin

Word Map on EC 3.4.23.40
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
3.4.23.40
-
RECOMMENDED NAME
GeneOntology No.
Phytepsin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-/-Asp- and -Asp-/-Asp- bonds in 2S albumin from plant seeds
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
219715-98-7
not distinguished from other aspartic proteinases, i.e. Ec 3.4.23.x
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
rape
-
-
Manually annotated by BRENDA team
hemp
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
squash
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
buckwheat
-
-
Manually annotated by BRENDA team
sunflower
-
-
Manually annotated by BRENDA team
lotus
-
-
Manually annotated by BRENDA team
tobacco
-
-
Manually annotated by BRENDA team
rice
-
-
Manually annotated by BRENDA team
Jack pine
-
-
Manually annotated by BRENDA team
Scots pine
-
-
Manually annotated by BRENDA team
tomato
-
-
Manually annotated by BRENDA team
sorghum
-
-
Manually annotated by BRENDA team
cacao
-
-
Manually annotated by BRENDA team
Triticum durum x Haynaldia villosa
hybrid between Triticum durum and Hynaldia villosa
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
either the plant-specific insert domain or the C-terminal peptide VGFAEAA is necessary and sufficient to direct proteins to the vacuole. Both domains are vacuolar sorting determinants
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Acid denatured bovine hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
Albumin + H2O
?
show the reaction diagram
alpha-casein + H2O
?
show the reaction diagram
-
formation of two cleavage products of about 30 and 23 kDa
-
?
Barley lectin + H2O
?
show the reaction diagram
-
removal of 13 amino acids from the C-terminus
-
-
-
beta-casein + H2O
?
show the reaction diagram
-
formation of one single product of about 23 kDa
-
?
casein + H2O
?
show the reaction diagram
Edestin + H2O
?
show the reaction diagram
-
-
-
-
-
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
-
Gliadin + H2O
?
show the reaction diagram
Glucagon + H2O
?
show the reaction diagram
-
-
-
-
-
Hemoglobin + H2O
?
show the reaction diagram
Insulin B-chain + H2O
?
show the reaction diagram
-
-
-
-
-
kappa-casein + H2O
?
show the reaction diagram
-
digestion of kappa-casein results in the appearance of a product of about 16 kDa
-
?
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
L-Pro-L-Thr-L-Glu-L-Phe(p-NO2)-L-Phe-L-Arg-L-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe + H2O
?
show the reaction diagram
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu + H2O
-
show the reaction diagram
Lys-Pro-Ile-Glu-(4-nitro)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
-
-
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
?
show the reaction diagram
Melittin + H2O
?
show the reaction diagram
-
-
-
-
-
Pro-Pro-Thr-Ile-(4-nitro)Phe-Arg-Leu + H2O
?
show the reaction diagram
-
-
-
-
-
Protein + 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
Protein + H2O
?
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
diazoacetyl-norleucine methyl ester
;
Diazoacetylnorleucine methyl ester
-
-
H-256
-
substrate-analog inhibitor for cathepsin D
H-261
-
substrate-analog inhibitor for cathepsin D
L363 564
-
substrate-analog inhibitor for cathepsin D
Lactoyl-pepstatin
-
-
-
Pepstatin
pepstatin A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
-
37°C, pH 7.4
0.07
L-Pro-L-Thr-L-Glu-L-Phe(p-NO2)-L-Phe-L-Arg-L-Leu
-
pH 5.0
0.081 - 0.64
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe
-
0.108 - 0.11
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu
-
0.375
Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65
L-Lys-L-Pro-L-Ala-L-Glu-L-Phe-L-Phe(NO2)-L-Ala-L-Leu
Cynara cardunculus
-
37°C, pH 7.4
144
L-Pro-L-Thr-L-Glu-L-Phe(p-NO2)-L-Phe-L-Arg-L-Leu
Cynara cardunculus var. scolymus
-
pH 5.0
13.7 - 86.2
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe
-
55.63 - 89.4
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.3 - 1066
Leu-Ser-Phe(NO2)-Ahx-Ala-Leu-OMe
206885
515.1 - 808.3
Lys-Pro-Ala-Glu-Phe-Phe-Phe(NO2)-Ala-Leu
206886
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001 - 0.00003
Pepstatin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.703
-
substrate gliadin
91.8
pH 4.7, 37°C; pH 4.7, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 3
-
substrate casein
2.2
-
substrates albumin, fibrin
2.4 - 3.8
-
substrates casein, hemoglobin
2.5 - 4.2
-
substrates casein, hemoglobin
2.5 - 3.5
-
substrate hemoglobin
3.1
Triticum durum x Haynaldia villosa
-
chromophoric peptide substrate
3.2
-
substrate hemoglobin
3.3
-
substrate Lys-Pro-Ile-Glu-Phe-(4-nitro)Phe-Arg-Leu
3.5 - 3.9
-
substrate hemoglobin
3.5
-
substrate hemoglobin
3.7 - 4.1
-
chromophoric peptide substrate
3.7
-
substrate hemoglobin
4.3
-
substrate edestin
5.1
-
substrate casein
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
about 40% of maximum activity
4
-
inactive above
7
-
about 10% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
isoform cynarase A
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.2
-
isoelectric focusing, cynarase A
3.3
-
isoelectric focusing, cynarase B
3.4
-
isoelectric focusing, cynarase C
5.7
calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9000
-
1 * 29000 + 1 * 9000, SDS-PAGE
11500
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
13300
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
15000
x * 31000, and x * 15000, SDS-PAGE; x * 34000, and x * 15000, SDS-PAGE
20000
-
ultracentirfugation
26000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
28000
-
gel filtration
29700
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
31000
x * 31000, and x * 15000, SDS-PAGE
32000
-
1 * 32000 + 1 * 16000 (48-kDa aspartic proteinase, precursor of the 40-k-Da aspartic proteinase), 1 * 29000 + 1 * 11000 (40-k-Da aspartic proteinase), SDS-PAGE
32300
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
34500
-
1 * 29700 + 1 * 13300, cynarase A, 1 * 34500 + 1 * 11500, cynarase B, 1 * 32300 + 1 * 13300, cynarase C, SDS-PAGE
36000 - 37000
-
ultracentrifugation, gel filtration
36000 - 40000
-
gel filtration
39000
-
PAGE
40000 - 42000
40000
-
2 * 40000, sequence of cDNA
40800
-
gel filtration, cynarase A
43400
-
gel filtration, cynarase B
46000
-
gel filtration, cynarase C
47000
-
x * 47000, and x * 37000, processing intermediates, x * 26000 + x * 11000, associated by disulfide bridge, mature enzyme, SDS-PAGE
50000
-
seeds, gel filtration
52600
x * 37000, SDS-PAGE, mature enzyme. x * 52600, calculated for proenzyme
55230
x * 55230, calculated
58000
-
1 * 58000, SDS-PAGE
59000
-
gel filtration
60000 - 65000
-
gel filtration
60500
-
gel filtration
66000
Triticum durum x Haynaldia villosa
-
gel filtration
66500
-
1 * 66500, SDS-PAGE
89000
-
leaf, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.72 A resoultion. Structure includes two molecules, built up by two glycosylated peptide chains of 31 and 15 kDa. The glycosyl content is described by 19 sugar rings attached to residues Asn67 and Asn257 localized on the molecular surface away from the conserved active site. A hydrogen bond between Gln126 and Manbeta4 renders the monosaccharide oxygen O2 sterically inaccessible to accept a xylosyl residue, explaining a hitherto unknown type of plant glycan. The Arg-Gly-Asp sequence, involved in recognition of a putative cardosin A receptor, is found in a loop between two beta-strands on the molecular surface opposite the active site cleft
-
analysis of solvent structure in crystals, comparison of aspartic proteases, zymogen form
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
at least 24 h at 37°C
30849
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
pH 4.0-8.0, at least 24 h stable
40
5 h, 80% residual activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4¦C, stable for 2 or more weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from stigma, isoform cynarase a, cynarase B, and cynarase C
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Kluyveromyces lactis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression under postharvest chilling treatment in two pineapple varieties differing in their resistance to blackheart development reveals opposite trends. The resistant variety shows an up-regulation of AP1 precursor gene expression whereas the susceptible shows a down-regulation in response to postharvest chilling treatment. The same trend is observed regarding specific aspartic protease enzyme activity in both varieties
optimization of culture conditions for expression in Kluyveromyces lactis, best conditions are YPGal 4% for 120 h at 30°C. Subjecting the precursor form to a protein engineering approach followed by codon optimization leads to a clear improvement in the production of the protease, which also results in a reduction in expression time
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D32A
-
active site mutant, inactive, no processing of proenzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry