3.4.24.B36: Vipera ammodytes ammodytes metalloproteinase VaH1

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For detailed information about Vipera ammodytes ammodytes metalloproteinase VaH1, go to the full flat file.

Reaction

Hydrolyzes the alpha-chain of human fibrinogen. The enzyme hydrolyzes most rapidly the peptide bond between Ala14 and Lys156 followed by Tyr16-/-Leu17 and His10-/-Leu11 at much slower rates. Strong hemorrhagic activity =

Synonyms

VaH1

ECTree

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.24 Metalloendopeptidases

3.4.24.B36 Vipera ammodytes ammodytes metalloproteinase VaH1

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Results	in table
1	AA Sequence
2	Inhibitors
1	Molecular Weight [Da]
1	Organism
1	pH Optimum
1	pI Value
1	Posttranslational Modification
1	Purification (Commentary)
2	Reaction
1	Reference
1	Source Tissue
4	Substrates and Products (Substrate)
1	Subunits
1	Synonyms

Reference

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Reference on EC 3.4.24.B36 - Vipera ammodytes ammodytes metalloproteinase VaH1

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732947

Leonardi, A.; Gubensek, F.; Krizaj, I.

Purification and characterisation of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes

Toxicon

55-62

2002

Vipera ammodytes ammodytes (P0DJ44)

11602279