Information on EC 3.4.24.36 - leishmanolysin

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.36
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RECOMMENDED NAME
GeneOntology No.
leishmanolysin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-/-Leu-Lys-Lys-
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
161052-06-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
LRC-L119
SwissProt
Manually annotated by BRENDA team
LV39
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain P07, isolated from an opossum, Didelphis albiventris
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Manually annotated by BRENDA team
strain P07, isolated from an opossum, Didelphis albiventris
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
show the reaction diagram
azocasein + H2O
?
show the reaction diagram
azocasein + H2O
low molecular weight acid-soluble azopeptides
show the reaction diagram
Bovine serum albumin + H2O
?
show the reaction diagram
casein + H2O
?
show the reaction diagram
Casein micelles + H2O
?
show the reaction diagram
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milk assay
-
-
-
Dansyl-Ala-Tyr-Leu-Lys-Lys-Trp-Val-NH2 + H2O
Dansyl-Ala-Tyr + ?
show the reaction diagram
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cleavage site: Tyr-Leu
-
-
Elastin + H2O
?
show the reaction diagram
-
zymographic assay
-
-
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Fibrinogen + H2O
?
show the reaction diagram
Gelatin + H2O
?
show the reaction diagram
Glucagon + H2O
?
show the reaction diagram
Hemoglobin + H2O
?
show the reaction diagram
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
show the reaction diagram
Leu-Ile-Ala-Tyr-Ser-Lys-Lys-Ala-Thr + H2O
?
show the reaction diagram
MARCKS-related protein MRP + H2O
?
show the reaction diagram
myristoylated alanine-rich C kinase substrate MARCKS + H2O
?
show the reaction diagram
Oxidized insulin B-chain + H2O
?
show the reaction diagram
p130Cas + H2O
?
show the reaction diagram
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phosphorylated adaptor protein of fibroblasts
-
-
?
Peptide 170-182 from CW-3 HLA antigen + H2O
?
show the reaction diagram
Peptide 83-94 from beta-chain of HLA DO + H2O
?
show the reaction diagram
Peptide 97-105 from Leishmanolysin + H2O
?
show the reaction diagram
Peptides from horse cytochrome c + H2O
?
show the reaction diagram
protein tyrosine phosphatase PTP1B + H2O
?
show the reaction diagram
protein tyrosine phosphatase SHP-1 + H2O
?
show the reaction diagram
protein tyrosine phosphatase TCPTP + H2O
?
show the reaction diagram
protein-tyrosine phosphatase-PEST + H2O
?
show the reaction diagram
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fibroblast protein cleaved upon infection by Leishmania major. cleavage augments its catalytic activity. Cleavage occurs likely near its C-terminal nuclear localization signal. Removal of the nuclear localization signal could allow the phosphatase to access additional substrates and also enhance its catalytic activity
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-
?
transcription factor AP-1 + H2O
?
show the reaction diagram
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inactivation and degradation
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-
?
additional information
?
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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 tyrosine phosphatase PTP1B + H2O
?
show the reaction diagram
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activation and posttranslationally modification of host enzymes in infected macrophages. The PTP1B cleavage fragments are enzymatically active. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63
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-
?
protein tyrosine phosphatase SHP-1 + H2O
?
show the reaction diagram
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activation and posttranslationally modification of host enzymes in infected macrophages. The SHP-1 cleavage fragments are enzymatically active
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-
?
protein tyrosine phosphatase TCPTP + H2O
?
show the reaction diagram
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activation and posttranslationally modification of host enzymes in infected macrophages. The TCPTP cleavage fragments are enzymatically active
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-
?
transcription factor AP-1 + H2O
?
show the reaction diagram
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inactivation and degradation
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-bipyridyl
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strong, Zn2+ reverses, bovine serum albumin as substrate
2-mercaptoethylamine
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Zn2+ reverses, bovine serum albumin as substrate
8-hydroxyquinoline
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Zn2+ reverses, bovine serum albumin as substrate
Benzyloxycarbonyl-Tyr-Leu-NHOH
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i.e. hydroxamate-derivatized dipeptide, strong, azocasein as substrate
EDTA
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strong, Zn2+ reverses, bovine serum albumin as substrate
EGTA
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strong, Zn2+ reverses, bovine serum albumin as substrate
thioglycolic acid
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Zn2+ reverses, bovine serum albumin as substrate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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possible autocatalytic mechanism for activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037 - 0.011
casein
20
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1 - 12.7
casein
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
300 - 3200
casein
738
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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promastigote enzyme
4.7 - 4.8
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assay at
5.5
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amastigote MSPS
5.5 - 6
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soluble amastigote enzyme, Leishmania mexicana
6 - 8
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promastigote MSPS
7 - 8.5
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Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr as substrate
7.5 - 10
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azocasein as substrate
additional information
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isoelectric pattern, microheterogeneity in MW and charge
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7 - 11.7
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about half-maximal activity at pH 4.7 and 11.7, azocasein as substrate
5.3 - 9.5
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about half-maximal activity at pH 5.3 and 9.5, Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr as substrate
additional information
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the surface metallopeptidase is active at a broad spectrum of pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.65
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MSPS and MSPL
5.8 - 6.7
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8 different bands of isozymes within this range
additional information
pI-values of isoforms from stationary phase are 5.2 to 6.1
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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GP63 is able to act on its substrate proteins within the nucleus of its host cell
Manually annotated by BRENDA team
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Leishmania mexicana amastigotes
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Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51674
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
51689
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
52000
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x * 52000, Leishmania major, deglycosylated enzyme, x * 53200, Leishmania major, deglycosylated enzyme, SDS-PAGE
52570
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Leishmania major, calculated from nucleotide sequence plus carbohydrate core of GPI anchor
53200
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x * 52000, Leishmania major, deglycosylated enzyme, x * 53200, Leishmania major, deglycosylated enzyme, SDS-PAGE
59177
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
62950
x * 62950, calculated
63000
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SDS-PAGE
66000
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x * 66000, SDS-PAGE
additional information
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microheterogeneity in MW and charge
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
posttranslational modifications of enzyme isoforms include N-glycosylation, GPI anchor addition and phosphorylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling based on the strucuture of Leishmania major gp63. The protein consists of the N-terminal, central and C-terminal domain
Leishmania major, crystallographic parameters
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molecular dynamics simulation of enzyme in water. Upon solvation, enzyme undergoes a sharp structural relaxation with respect to the crystal structure. Fingerprint fluctuations of enzyme are characterized by the motion of a large part of the N-terminal domain, which is also involved in substrate recognition and proenzyme activation. Residues involved in interdomain binding are highly conserved
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monoclinic crystals, space group C2 with a : 107.2 A, b : 90.6 A, c : 70.6 A, and tetragonal crystals, space group P4(1)2(1)2(1), a : b : 63.6 A, c : 251.4 A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
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at least 30 min stable
31227
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Resistant to proteolytic degradation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 mg enzyme/ml, in 10 mM Tris-HCl buffer, pH 8, 0.02% w/v NaN3, prolonged periods of time
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
lipophosphoglycan deficient LRC-L119 promastigotes
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native enzyme from promastigotes by immunoprecipitation
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promastigotes, monoclonal affinity purification
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recombinant enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and ultrafiltration
recombinant His-tagged full-length gp63 from Escherichia coli BL21 (DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
construction of full-length gp63 gene in mammalian pcDNA3.1 (2/2) expression vector, expression in CHO cells and of His-tagged protein in Escherichia coli BL21 (DE3) pLysS
DNA and amino acid sequence determination, analysis and comparison, overexpression in Escherichia coli strain BL21 (DE3) pLysS
expressed in Escherichia coli JM109(DE3)
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expression in Escherichia coli
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genes gp63, DNA and amino acid sequence determination and analysis, sequence analysis and identification of homologues of major surface protease genes and sequence comparisons, phylogenetic analysis
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F448V
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F448Y
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
S446A
site-directed mutagenesis, the mutant shows 50% reduced activity and altered kinetics compared to the wild-type enzyme
S446T
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F448V
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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F448Y
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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S446A
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site-directed mutagenesis, the mutant shows 50% reduced activity and altered kinetics compared to the wild-type enzyme
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S446T
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
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