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Literature summary for 2.7.7.1 extracted from

  • Contreras Rodriguez, L.E.; Ziegler, M.; Ramirez Hernandez, M.H.
    Kinetic and oligomeric study of Leishmania braziliensis nicotinate/nicotinamide mononucleotide adenylyltransferase (2020), Heliyon, 6, e03733 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Leishmania braziliensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1789
-
 nicotinamide ribonucleotide pH 7.4, 20°C Leishmania braziliensis
3.5
-
 ATP pH 7.4, 20°C Leishmania braziliensis
166.6
-
 diphosphate pH 7.4, 20°C Leishmania braziliensis
412.2
-
 NAD+ pH 7.4, 20°C Leishmania braziliensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41980
-
 gel filtration, recombinant His-tagged protein Leishmania braziliensis

Organism

Organism UniProt Comment Textmining
Leishmania braziliensis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + nicotinamide ribonucleotide
-
 Leishmania braziliensis diphosphate + NAD+
-
 r
diphosphate + NAD+
-
 Leishmania braziliensis ATP + nicotinamide ribonucleotide
-
 r
additional information bifunctional enzyme, additionally catalyzes the reaction with nicotinate ribonucleotide, reaction of EC 2.7.7.18 Leishmania braziliensis ?
-
-

Subunits

Subunits Comment Organism
monomer 1 * 36000, calculated from sequence Leishmania braziliensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.1
-
 ATP pH 7.4, 20°C Leishmania braziliensis
0.2
-
 nicotinamide ribonucleotide pH 7.4, 20°C Leishmania braziliensis
11.2
-
 diphosphate pH 7.4, 20°C Leishmania braziliensis
16.6
-
 NAD+ pH 7.4, 20°C Leishmania braziliensis