Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

EC Number Activating Compound Comment Organism Structure
3.4.24.B35 glycosaminoglycan proteolytic activity of the enzyme depends on the presence of glycosaminoglycans Vipera ammodytes ammodytes

Application

EC Number Application Comment Organism
3.4.24.B35 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

EC Number General Stability Organism
3.4.24.B35 stability of the enzyme depends on Zn2+ and Ca2+ ions and on the presence of glycosaminoglycans Vipera ammodytes ammodytes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B35 Ca2+ the proteolytic activity of the enzyme depends on Zn2+ and Ca2+ ions Vipera ammodytes ammodytes
3.4.24.B35 Zn2+ the proteolytic activity of the enzyme depends on Zn2+ and Ca2+ ions Vipera ammodytes ammodytes

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.B35 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
3.4.24.B35 110200
-
 MALDI/TOF mass spectrometry Vipera ammodytes ammodytes
3.4.24.B35 130000
-
 SDS-PAGE under non-reducing conditions Vipera ammodytes ammodytes

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B35 Vipera ammodytes ammodytes V5TBK6
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.B35 glycoprotein N-deglycosylation reduces the mass of each monomer by 8.7 kDa Vipera ammodytes ammodytes

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B35
-
 Vipera ammodytes ammodytes

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B35 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
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.B35 venom
-
 Vipera ammodytes ammodytes
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B35 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 ?
-
 ?
3.4.24.B35 bovine fibronectin + H2O degraded intensively Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B35 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 ?
-
 ?
3.4.24.B35 human collagen IV + H2O degraded slightly Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B35 human fibrinogen alpha-chain + H2O powerful alpha-fibrinogenase, hydrolysis at Glu422-/-Leu423 and Glu520-/-Phe521 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B35 human fibrinogen beta-chain + H2O hydrolysed only partially at Lys22-/-Arg23 and Pro28-Leu29 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B35 Insulin B-chain + H2O the enzyme cleaves Tyr16-Leu17 preferentially, followed by Gln4-His5 and His10-Leu11 Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B35 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 ?
-
 ?
3.4.24.B35 murine laminin + H2O degraded slightly Vipera ammodytes ammodytes ?
-
 ?
3.4.24.B35 Nidogen + H2O two cleavage positions: Ser322-/-Phe323 and Tyr352-/-Asn353 Vipera ammodytes ammodytes ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B35 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

EC Number Synonyms Comment Organism
3.4.24.B35 hemorrhagin VaH4
-
 Vipera ammodytes ammodytes

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.B35 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

EC Number Organism Comment pI Value Maximum pI Value
3.4.24.B35 Vipera ammodytes ammodytes appears in numerous isoforms with pIs spanning from 5.5 to 7.5, isoelectric focussing 7.5 5.5