Information on EC 3.4.24.52 - trimerelysin I

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The expected taxonomic range for this enzyme is: Trimeresurus flavoviridis

EC NUMBER
COMMENTARY
3.4.24.52
-
RECOMMENDED NAME
GeneOntology No.
trimerelysin I
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cleavage of only two bonds His10-/-Leu and Ala14-/-Leu in the insulin B chain
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Hemorrhagic metalloproteinase HR1A
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-
-
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Hemorrhagic proteinase HR1A
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-
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Metalloproteinase HR1A
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metalloproteinase HR1b
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Trimeresurus metalloendopeptidase I
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CAS REGISTRY NUMBER
COMMENTARY
151125-16-5
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
formerly Trimeresurus flavoviridis
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Aminobenzoyl-Ala-Gly-Leu-Ala-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Ala-Gly + Leu-Ala-2,4-dinitroanilinoethylamide
show the reaction diagram
-
peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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-
2-Aminobenzoyl-Asn-Ala-Pro-Leu-Ala-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Asn-Ala-Pro + Leu-Ala-2,4-dinitroanilinoethylamide
show the reaction diagram
-
peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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2-Aminobenzoyl-Gly-Phe-Arg-Leu-Leu-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Gly-Phe-Arg + Leu-Leu-2,4-dinitroanilinoethylamide
show the reaction diagram
-
peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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-
2-Aminobenzoyl-Phe-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Phe-Ser-Pro + Met-Leu-2,4-dinitroanilinoethylamide
show the reaction diagram
-
peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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-
2-Aminobenzoyl-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Ser-Pro + Met-Leu-2,4-dinitroanilinoethylamide
show the reaction diagram
-
peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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-
2-Aminobenzoyl-Thr-Glu-Lys-Leu-Val-2,4-dinitroanilinoethylamide + H2O
2-Aminobenzoyl-Thr-Glu-Lys + Leu-Val-2,4-dinitroanilinoethylamide
show the reaction diagram
-
peptide synthesized on the basis of sequences close to autoproteolysis cleavage sites, fluorogenic substrate
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casein + H2O
?
show the reaction diagram
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-
?
casein + H2O
?
show the reaction diagram
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enzyme form HR1A, very poor substrate for HR1B
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insulin B chain + H2O
?
show the reaction diagram
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?
Insulin B-chain derived peptide C + H2O
?
show the reaction diagram
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i.e. fragment Phe1-Ala14, cleavage site: His10-Leu11, poor substrate
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Metalloproteinase HR1A + H2O
Hydrolyzed metalloproteinase HR1A
show the reaction diagram
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MW 60000, bears autoproteolytic activity which is suppressed by more than 0.005 mM Ca2+ or 0.05 mM EDTA
fragment MW 32000 from COOH-terminus and low MW fragments
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Oxidized insulin B-chain + H2O
Peptide C + peptide D + peptide A + peptide B
show the reaction diagram
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rapid hydrolysis, cleavage sites: Ala14-Leu15 and His10-Leu11, the former bond is more rapidly cleaved than the latter, no cleavage of His5-Leu6
i.e. fragments Phe1-Ala14, Leu15-Ala30, Leu11-Ala14 and Phe1-His10
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Metalloproteinase HR1B + H2O
Hydrolyzed metalloproteinase HR1B
show the reaction diagram
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MW 60000, bears autoproteolytic activity which is suppressed by more than 5 mM Ca2+ or EDTA
fragment MW 34000 and low MW fragments
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additional information
?
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2-aminobenzoyl-Asn-Ala-Pro-Ser-Ala-2,4-dinitroanilinoethylamide, 2-aminobenzoyl-Ala-Thr-Asp-Ile-Val-2,4-dinitroanilinoethylamide, 2-aminobenzoyl-Gly-Phe-Arg-Leu-2,4-dinitroanilinoethylamide, 2-aminobenzoyl-Gly-Phe-Leu-Gly-Pro-2,4-dinitroanilinoethylamide
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additional information
?
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no substrates are insulin B-chain derived peptide D (fragment Leu15-Ala30)
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additional information
?
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the major hemorrhagic component in the venom of Trimeresurus flavoviridis
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additional information
?
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high molecular mass hemorrhagic metalloproteinase
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additional information
?
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the enzyme shows strong hemorrhagic activity
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additional information
?
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substrate specificity differs from that of enzyme metalloproteinase HR1b, substrate D-Nbeta-(2-(N-methylamino)benzoyl)-2,3-diaminopropionic acid-glycine-Zaa-Yaa-Xaa-alanine-phenylalanine-proline-(2,4-dinitrophenyl)-lysine-D-arginine-D-arginine. Xaa stands for 19 natural amino acids (excluding cysteine). Yaa stands for 5 natural amino acids (proline, tyrosine, lysine, isoleucine and asparagine). Zaa stands for another 5 amino acids (phenylalanine, alanine, valine, glutamine and arginine). HR1a preferres alanine, histidine, proline, methionine, and tyrosine in descending order at Xaa position and valine and aspartic acid at the Yaa and Zaa positions respectively. measured by fluorescence resonance energy transfer
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-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the major hemorrhagic component in the venom of Trimeresurus flavoviridis
-
-
-
additional information
?
-
-
high molecular mass hemorrhagic metalloproteinase
-
-
-
additional information
?
-
-
the enzyme shows strong hemorrhagic activity
-
-
-
additional information
?
-
-
substrate specificity differs from that of enzyme metalloproteinase HR1b
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-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
metalloproteinase; the amino-terminal half of enzyme form HR1B represents a metalloproteinase structure similar to the low MW metalloproteinases HR2a, H2-proteinase and hemorrhagic toxin d
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
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inhibits the hemorrhagic and proteolytic activity of HR1A
EDTA
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inhibits the hemorrhagic and proteolytic activity of HR1A
additional information
-
specific monoclonal human antibodies HuMAbs neutralize the HR1a, determined by in vitro neutralization assay and by neutralization of the hemorrhagic activity, overview, from hybridoma from the fusion of SP2/0-Ag14 myeloma cells and spleen cells from KM mice immunized with purified HR1a, epitope mapping, overview
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
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2-Aminobenzoyl-Ala-Gly-Leu-Ala-2,4-dinitroanilinoethylamide
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-
0.014
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2-aminobenzoyl-Asn-Ala-Phe-Leu-Ala-2,4-dinitroanilinoethylamide
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-
0.013
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2-Aminobenzoyl-Phe-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide
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2-aminobenzoyl-Gly-Phe-Arg-Leu-Leu-2,4-dinitroanilinoethylamide
0.015
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2-Aminobenzoyl-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide
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0.0076
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2-Aminobenzoyl-Thr-Glu-Lys-Leu-Val-2,4-dinitroanilinoethylamide
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SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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-
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
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2-aminobenzoyl-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide as substrate
additional information
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pI: 4.4
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10.5
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half-maximal activity at pH 6 and 10.5, 2-aminobenzoyl-Ser-Pro-Met-Leu-2,4-dinitroanilinoethylamide as substrate
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
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assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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amino acid composition
additional information
-
-
amino acid sequence of HR1B protein
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 60000, Trimeresurus flavoviridis, SDS-PAGE
additional information
-
molecular modeling of the three-dimensional structure of the HR1a, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
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contains neutral sugar, amino sugar and sialic acid amounting to 17-18% on total weight basis
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
two immunologically closely related enzyme forms, HR1A and HR1B
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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causes localized hemorrhage through the degradation of basement membrane