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

BRENDA support

Literature summary extracted from

  • Kuhn, I.; Kellenberger, E.; Schuber, F.; Muller-Steffner, H.
    Schistosoma mansoni NAD+ catabolizing enzyme: identification of key residues in catalysis (2013), Biochim. Biophys. Acta, 1834, 2520-2527.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.2.5 recombinant expression of His-tagged wild-type and mutant enzymes in Pichia apstoris and secretion to the culture medium Schistosoma mansoni

Protein Variants

EC Number Protein Variants Comment Organism
3.2.2.5 D133A site-directed mutagenesis Schistosoma mansoni
3.2.2.5 E124A site-directed mutagenesis, the mutant is not inhibited by cyanidin in contrast to the wild-type enzyme Schistosoma mansoni
3.2.2.5 E202A site-directed mutagenesis, the mutant is much less inhibited by cyanidin compared to the wild-type enzyme Schistosoma mansoni
3.2.2.5 H103A site-directed mutagenesis, the mutant is less inhibited by cyanidin compared to the wild-type enzyme Schistosoma mansoni
3.2.2.5 H103F site-directed mutagenesis Schistosoma mansoni
3.2.2.5 S169A site-directed mutagenesis Schistosoma mansoni
3.2.2.5 W165A site-directed mutagenesis, the mutant is inhibited by cyanidin like the wild-type enzyme Schistosoma mansoni
3.2.2.5 W165F site-directed mutagenesis Schistosoma mansoni

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.5 cyanidin complete inhibition of the wild-type enzyme at 0.1 mM Schistosoma mansoni

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.5 additional information
-
 additional information steady-state kinetics Schistosoma mansoni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.5 NAD+ + H2O Schistosoma mansoni
-
 ADP-D-ribose + nicotinamide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.5 Schistosoma mansoni Q32TF5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.5 recombinant His-tagged wild-type and mutant enzymes from Pichia apstoris culture supernatant by nickel affinity chromatography Schistosoma mansoni

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.5 NAD+ + H2O
-
 Schistosoma mansoni ADP-D-ribose + nicotinamide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.2.5 NAD+ catabolizing enzyme
-
 Schistosoma mansoni
3.2.2.5 SmNACE
-
 Schistosoma mansoni

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.5 37
-
 assay at Schistosoma mansoni

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.5 5.5
-
 assay at Schistosoma mansoni

General Information

EC Number General Information Comment Organism
3.2.2.5 evolution the enzyme shows significant structural and functional analogy to the members of the CD38/ADP-ribosyl cyclase family but a lack of ADP-ribosyl cyclase activity that might be ascribed to subtle changes in its active site. In sharp contrast with mammalian CD38, the signature Glu124 is as critical as Glu202 for catalysis by the parasite enzyme. Sequence comparisons Schistosoma mansoni
3.2.2.5 additional information three dimensional homology modeling of the enzyme, very important role of Glu202 and of the hydrophobic domains overwhelmingly in the efficiency of the nicotinamide-ribosyl bond cleavage step. The nicotinamide-ribosyl bond is cleaved upon the first step of catalysis and is surrounded by three hydrophobic side chains Leu123, Tyr172 and Phe102 Schistosoma mansoni