Information on EC 3.4.24.B35 - Vipera ammodytes ammodytes metalloproteinase VaH4

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The expected taxonomic range for this enzyme is: Vipera ammodytes ammodytes

EC NUMBER
COMMENTARY hide
3.4.24.B35
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
Vipera ammodytes ammodytes metalloproteinase VaH4
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Glu422-/-Leu423 and Glu520-/-Phe521 bond of alpha-chain of human fibrinogen. Fibrinogen beta-chain is hydrolysed only partially at Lys22-/-Arg23 and Pro28-Leu29. In insulin B-chain the enzyme preferentially cleaves Tyr16-/-Leu17, followed by Gln4-/-His5 and His10-/-Leu11
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bovine factor X + H2O
?
show the reaction diagram
the major products of proteolysis of factor X by the enzyme are in the mass range from 33 to 45 kDa. Their N-terminal residues correspond to cleavage at residues 17, 20 and 22 upstream of the N-terminus of the heavy chain FXa
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-
?
bovine fibronectin + H2O
?
show the reaction diagram
degraded intensively
-
-
?
bovine prothrombin + H2O
?
show the reaction diagram
the enzyme does not activate prothrombin in vitro. After 1 h of incubation a weak band at 70 kDa is observed, which is not further hydrolysed if incubation is extended to 24 h. The enzyme cleaves prothrombin at Ser157-/-Gly158, releasing fragment 1 of activation peptide and prethrombin 1
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-
?
human collagen IV + H2O
?
show the reaction diagram
degraded slightly
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-
?
human fibrinogen alpha-chain + H2O
?
show the reaction diagram
powerful alpha-fibrinogenase, hydrolysis at Glu422-/-Leu423 and Glu520-/-Phe521
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-
?
human fibrinogen beta-chain + H2O
?
show the reaction diagram
hydrolysed only partially at Lys22-/-Arg23 and Pro28-Leu29
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-
?
Insulin B-chain + H2O
?
show the reaction diagram
the enzyme cleaves Tyr16-Leu17 preferentially, followed by Gln4-His5 and His10-Leu11
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-
?
murine laminin + H2O
?
show the reaction diagram
degraded slightly
-
-
?
Nidogen + H2O
?
show the reaction diagram
two cleavage positions: Ser322-/-Phe323 and Tyr352-/-Asn353
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-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
the proteolytic activity of the enzyme depends on Zn2+ and Ca2+ ions
Zn2+
the proteolytic activity of the enzyme depends on Zn2+ and Ca2+ ions
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycosaminoglycan
proteolytic activity of the enzyme depends on the presence of glycosaminoglycans
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
appears in numerous isoforms with pIs spanning from 5.5 to 7.5, isoelectric focussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
1 * 65000 (VaH4-A) + 1 * 65000 (VaH4-B), covalent dimer of two homologous subunits, VaH4-A and VaH4-B. Cys132 is involved in the inter-subunit disulfide bond
110200
MALDI/TOF mass spectrometry
130000
SDS-PAGE under non-reducing conditions
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
1 * 65000 (VaH4-A) + 1 * 65000 (VaH4-B), covalent dimer of two homologous subunits, VaH4-A and VaH4-B. Cys132 is involved in the inter-subunit disulfide bond
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
N-deglycosylation reduces the mass of each monomer by 8.7 kDa
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
stable between pH 5 and 8. Its stability over this pH range decreases substantially in the presence of imidazole and glycine, and in the absence of Ca2+ and Zn2+ ions. Addition to the buffer of glycosaminoglycans, chondroitin sulfate, dermatan sulfate or hyaluronic acid, at nanomolar concentrations, increases the stability of the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability of the enzyme depends on Zn2+ and Ca2+ ions and on the presence of glycosaminoglycans
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the enzyme displays a cytotoxic effect on cancer cells in culture, which makes it interesting for further medically-oriented studies