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Literature summary for 3.4.23.15 extracted from

  • Wilkinson, M.C.; Nightingale, D.J.H.; Harrison, R.A.; Wagstaff, S.C.
    Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom (2017), Toxicon, 137, 92-94 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
pepstatin A almost complete inhibition at 0.01 mM Echis ocellatus

Organism

Organism UniProt Comment Textmining
Echis ocellatus
-
saw-scaled viper
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Echis ocellatus

Purification (Commentary)

Purification (Comment) Organism
Mono Q column chromatography and phenyl Superose column chromatography Echis ocellatus

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Echis ocellatus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human angiotensinogen + H2O DRVYIHPFHLVIHN Echis ocellatus angiotensin I + VIHN
-
?
additional information the enzyme possesses no general protease activity Echis ocellatus ?
-
?
porcine angiotensinogen + H2O DRVYIHPFHLLVYS Echis ocellatus angiotensin I + angiotensinogen propeptide
-
?

Subunits

Subunits Comment Organism
? x * 42000, SDS-PAGE Echis ocellatus

Synonyms

Synonyms Comment Organism
SVAP
-
Echis ocellatus
SVAP A1 isoform Echis ocellatus
SVAP B1 isoform Echis ocellatus
SVAP B2 isoform Echis ocellatus
venom aspartic protease
-
Echis ocellatus