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Literature summary for 3.4.24.B35 extracted from

  • Leonardi, A.; Sajevic, T.; Kovacic, L.; Pungercar, J.; Lang Balija, M.; Halassy, B.; Trampus Bakija, A.; Krizaj, I.
    Hemorrhagin VaH4, a covalent heterodimeric P-III metalloproteinase from Vipera ammodytes ammodytes with a potential antitumour activity (2013), Toxicon, 77, 141-155.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
glycosaminoglycan proteolytic activity of the enzyme depends on the presence of glycosaminoglycans Vipera ammodytes ammodytes

Application

Application Comment Organism
medicine the enzyme displays a cytotoxic effect on cancer cells in culture, which makes it interesting for further medically-oriented studies Vipera ammodytes ammodytes

General Stability

General Stability Organism
stability of the enzyme depends on Zn2+ and Ca2+ ions and on the presence of glycosaminoglycans Vipera ammodytes ammodytes

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the proteolytic activity of the enzyme depends on Zn2+ and Ca2+ ions Vipera ammodytes ammodytes
Zn2+ the proteolytic activity of the enzyme depends on Zn2+ and Ca2+ ions Vipera ammodytes ammodytes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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 Vipera ammodytes ammodytes
110200
-
MALDI/TOF mass spectrometry Vipera ammodytes ammodytes
130000
-
SDS-PAGE under non-reducing conditions Vipera ammodytes ammodytes

Organism

Organism UniProt Comment Textmining
Vipera ammodytes ammodytes V5TBK6
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein N-deglycosylation reduces the mass of each monomer by 8.7 kDa Vipera ammodytes ammodytes

Purification (Commentary)

Purification (Comment) Organism
-
Vipera ammodytes ammodytes

Reaction

Reaction Comment Organism Reaction ID
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 fibrinogen gamma-chain and fibrin are not hydrolyzed Vipera ammodytes ammodytes

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Vipera ammodytes ammodytes
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bovine factor X + H2O 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 Vipera ammodytes ammodytes ?
-
?
bovine fibronectin + H2O degraded intensively Vipera ammodytes ammodytes ?
-
?
bovine prothrombin + H2O 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 Vipera ammodytes ammodytes ?
-
?
human collagen IV + H2O degraded slightly Vipera ammodytes ammodytes ?
-
?
human fibrinogen alpha-chain + H2O powerful alpha-fibrinogenase, hydrolysis at Glu422-/-Leu423 and Glu520-/-Phe521 Vipera ammodytes ammodytes ?
-
?
human fibrinogen beta-chain + H2O hydrolysed only partially at Lys22-/-Arg23 and Pro28-Leu29 Vipera ammodytes ammodytes ?
-
?
Insulin B-chain + H2O the enzyme cleaves Tyr16-Leu17 preferentially, followed by Gln4-His5 and His10-Leu11 Vipera ammodytes ammodytes ?
-
?
additional information no hydrolysis of human fibrinogen gamma-chain. No hydrolysis of fibrin. Hemorrhagic activity of the enzyme is ascribed to its hydrolysis of components of the extracellular matrix, particularly fibronectin and nidogen, and of some blood coagulation proteins, in particular the alpha-chain of fibrinogen Vipera ammodytes ammodytes ?
-
?
murine laminin + H2O degraded slightly Vipera ammodytes ammodytes ?
-
?
Nidogen + H2O two cleavage positions: Ser322-/-Phe323 and Tyr352-/-Asn353 Vipera ammodytes ammodytes ?
-
?

Subunits

Subunits Comment Organism
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 Vipera ammodytes ammodytes

Synonyms

Synonyms Comment Organism
hemorrhagin VaH4
-
Vipera ammodytes ammodytes

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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 Vipera ammodytes ammodytes

pI Value

Organism Comment pI Value Maximum pI Value
Vipera ammodytes ammodytes appears in numerous isoforms with pIs spanning from 5.5 to 7.5, isoelectric focussing 7.5 5.5