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Literature summary for 2.4.2.30 extracted from

  • Ritter, H.; Koch-Nolte, F.; Marquez, V.E.; Schulz, G.E.
    Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat (2003), Biochemistry, 42, 10155-10162.
    View publication on PubMed
Search for more literature for 2.4.2.30

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of complexes between wild-type and two mutant enzymes (E189I and E189A) on the one hand and the substrate analogues beta-methylenethiazole-4-carboxamideadenine dinucleotide and NADH as well as the substrate NAD+ on the other Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E189A about 5200fold decrease in NAD+ hydrolysis activity Rattus norvegicus
E189I 20000fold decrease in NAD+ hydrolysis activity Rattus norvegicus
E189S about 5200fold decrease in NAD+ hydrolysis activity Rattus norvegicus
Q187A/E189A 50000fold decrease in NAD+ hydrolysis activity Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 NAD+ hydrolysis of NAD+, wild-type enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
 recombinant enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NAD+ + H2O
-
 Rattus norvegicus nicotinamide + ADP-ribose
-
 ?

Synonyms

Synonyms Comment Organism
ecto-ADP-ribosyltransferase 2.2
-
 Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0002
-
 NAD+ hydrolysis of NAD+, mutant enzyme Q187A/189A Rattus norvegicus
0.0005
-
 NAD+ hydrolysis of NAD+, mutant enzyme E189I Rattus norvegicus
0.002
-
 NAD+ hydrolysis of NAD+, mutant enzyme E189A Rattus norvegicus
0.002
-
 NAD+ hydrolysis of NAD+, mutant enzyme E189S Rattus norvegicus
12
-
 NAD+ hydrolysis of NAD+, wild-type enzyme Rattus norvegicus