Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.23.16 extracted from

  • Lentini, A.; Tabolacci, C.; Melino, S.; Provenzano, B.; Beninati, S.
    Post-translational modification of glutamine and lysine residues of HIV-1 aspartyl protease by transglutaminase increases its catalytic activity (2010), Biochem. Biophys. Res. Commun., 393, 546-550.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
transglutaminase incubation of HIV-1 aspartyl protease with transglutaminase increases its catalytic activity in a time- and concentration-dependent manner. Enzyme activity is increased, up to about 170% of control value, after 1 h incubation with 0.008 units of transglutaminase in the presence of Ca2+. The activation is completely abolished by spermidine Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Human immunodeficiency virus 1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Gag-Pol polyprotein + H2O Human immunodeficiency virus 1
-
?
-
?

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gag-Pol polyprotein + H2O
-
Human immunodeficiency virus 1 ?
-
?

Subunits

Subunits Comment Organism
homodimer
-
Human immunodeficiency virus 1

Synonyms

Synonyms Comment Organism
HIV-1 aspartyl protease
-
Human immunodeficiency virus 1
HIV-1 PR
-
Human immunodeficiency virus 1

General Information

General Information Comment Organism
physiological function the enzyme is required for virus replication Human immunodeficiency virus 1