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Literature summary for 3.4.21.19 extracted from

  • Srinivasulu, S.; Acharya, A.S.
    Product-conformation-driven ligation of peptides by V8 protease (2002), Protein Sci., 11, 1384-1392.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information mutations within the amino acid sequence alpha17-40 influence the organic co-solvent-induced conformation and concomittant resistance of E30-R31 peptide bond to cleavage occurs, alteration of the thermaldynamic stability of the splicedon, the flanking regions are involved in stabilization Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and thermodynamic stability Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Staphylococcus aureus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human hemoglobin + H2O slpicedon consisting of a flanking region FR1, the EALER sequence, and a flanking region FR2, splicing reaction at E30-R31, facilitated by organic co-solvent-induced secondary conformation of alpha17-40 within which the sequence EALER plays a major role Staphylococcus aureus ?
-
?
additional information splicing activity and specificity of the enzyme with complementary segments of human hemoglobin fragment alpha17-40, constructed by engineering of the primary structure, structural implications, overview Staphylococcus aureus ?
-
?

Synonyms

Synonyms Comment Organism
V8 protease
-
Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4
-
assay at Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Staphylococcus aureus