3.4.24.B35: Vipera ammodytes ammodytes metalloproteinase VaH4

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Reaction

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 =

Synonyms

hemorrhagin VaH4

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.B35 Vipera ammodytes ammodytes metalloproteinase VaH4

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Results	in table
1	Activating Compound
1	AA Sequence
1	Application
1	General Stability
2	Metals/Ions
3	Molecular Weight [Da]
1	Organism
1	pI Value
1	Posttranslational Modification
1	Purification (Commentary)
2	Reaction
1	Reference
1	Source Tissue
10	Substrates and Products (Substrate)
1	Subunits
1	Synonyms
1	Temperature Stability [°C]

Temperature Stability

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Temperature Stability on EC 3.4.24.B35 - Vipera ammodytes ammodytes metalloproteinase VaH4

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

58

Vipera ammodytes ammodytes

V5TBK6

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

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