Activating Compound | Comment | Organism | Structure |
---|---|---|---|
glycosaminoglycan | proteolytic activity of the enzyme depends on the presence of glycosaminoglycans | Vipera ammodytes ammodytes |
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 | Organism |
---|---|
stability of the enzyme depends on Zn2+ and Ca2+ ions and on the presence of glycosaminoglycans | Vipera ammodytes ammodytes |
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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Vipera ammodytes ammodytes | V5TBK6 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | N-deglycosylation reduces the mass of each monomer by 8.7 kDa | Vipera ammodytes ammodytes |
Purification (Comment) | Organism |
---|---|
- |
Vipera ammodytes ammodytes |
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 | Comment | Organism | Textmining |
---|---|---|---|
venom | - |
Vipera ammodytes ammodytes | - |
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 | 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 | Comment | Organism |
---|---|---|
hemorrhagin VaH4 | - |
Vipera ammodytes ammodytes |
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 |
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 |