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

Inhibitors

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

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

EDTA

Vipera ammodytes ammodytes

P0DJ44

eliminates the proteolytic as well as the hemorrhagic activity

732947

additional information

Vipera ammodytes ammodytes

P0DJ44

iodoacetamide, phenylmethylsulfonyl fluoride and pepstatin A, inhibitors of cysteine, serine and aspartic proteinases respectively, have no effect

732947

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