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Literature summary for 3.2.2.5 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)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Schistosoma mansoni Q32TF5
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
NAD+ catabolizing enzyme
-
Schistosoma mansoni
SmNACE
-
Schistosoma mansoni

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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
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