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Literature summary for 3.4.21.62 extracted from

  • Kennan, R.; Wong, W.; Dhungyel, O.; Han, X.; Wong, D.; Parker, D.; Rosado, C.; Law, R.; McGowan, S.; Reeve, S.; Levina, V.; Powers, G.; Pike, R.; Bottomley, S.; Ian Smith, A.; Marsh, I.; Whittington, R.; Whisstock, J.; Porter, C.; Rood, J.
    The subtilisin-like protease AprV2 is required for virulence and uses a novel disulphide-tethered exosite to bind substrates (2010), PLoS Pathog., 6, e1001210.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure shows that an unusual extended disulfhide-tethered loop functions as an exosite, mediating effective enzyme-substrate interactions. The disulphide bond and Tyr92, which is located at the exposed end of the loop, is functionally important Dichelobacter nodosus

Protein Variants

Protein Variants Comment Organism
DELTA83-99 truncation mutant is not functional Dichelobacter nodosus
Y92A mutant shows decreased elastin degradation Dichelobacter nodosus
Y92D mutant shows decreased elastin degradation Dichelobacter nodosus
Y92F mutant shows increased elastin degradation Dichelobacter nodosus
Y92L mutant shows decreased elastin degradation Dichelobacter nodosus

Organism

Organism UniProt Comment Textmining
Dichelobacter nodosus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta subunit of haemoglobin + H2O
-
Dichelobacter nodosus ?
-
?
Elastin + H2O
-
Dichelobacter nodosus ?
-
?
serum albumin + H2O
-
Dichelobacter nodosus ?
-
?
type I keratin + H2O
-
Dichelobacter nodosus ?
-
?

Synonyms

Synonyms Comment Organism
subtilisin-like protease AprV2
-
Dichelobacter nodosus

General Information

General Information Comment Organism
malfunction using a protease mutant of Dichelobacter nodosus it is shown in a sheep virulence model that AprV2 is required for virulence Dichelobacter nodosus