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Literature summary for 2.7.7.1 extracted from

  • Contreras, L.E.; Neme, R.; Ramirez, M.H.
    Identification and functional evaluation of Leishmania braziliensis nicotinamide mononucleotide adenylyltransferase (2015), Protein Expr. Purif., 115, 26-33.
    View publication on PubMed
Search for more literature for 2.7.7.1

Application

Application Comment Organism
pharmacology the amino-terminal insertion of Leishmania NMNATs as a promising pharmacological target for the development of specific control strategies Leishmania braziliensis

Cloned(Commentary)

Cloned (Comment) Organism
gene LBRM_17_1470 or lbnmnat, DNA and amino acid sequence determination and analysis, sequence comparisons, primary structure analysis reveals a Leishmania-specific amino-terminal insertion in NMNAT. The deletion of this insertion is negatively correlates with in vitro enzymatic activity. Recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Leishmania braziliensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method Leishmania braziliensis
0.15
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method Leishmania braziliensis
0.189
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method Leishmania braziliensis
0.755
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method Leishmania braziliensis
0.926
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method Leishmania braziliensis
0.985
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method Leishmania braziliensis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, best divalent cation Leishmania braziliensis
Mn2+ 42% of the activity with Mg2+ Leishmania braziliensis
additional information no activity with Ag+, Ca2+, or Cu2+ Leishmania braziliensis
Ni2+ 87% of the activity with Mg2+ Leishmania braziliensis
Zn2+ 9% of the activity with Mg2+ Leishmania braziliensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + nicotinamide ribonucleotide Leishmania braziliensis
-
 diphosphate + NAD+
-
 ?

Organism

Organism UniProt Comment Textmining
Leishmania braziliensis A4H990 gene LBRM_17_1470 or lbnmnat
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Leishmania braziliensis

Source Tissue

Source Tissue Comment Organism Textmining
promastigote
-
 Leishmania braziliensis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
28.22
-
 purified recombinant His-tagged enzyme, pH 7.4, 37°C Leishmania braziliensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + nicotinamide ribonucleotide
-
 Leishmania braziliensis diphosphate + NAD+
-
 ?

Synonyms

Synonyms Comment Organism
nicotinamide mononucleotide adenylyltransferase
-
 Leishmania braziliensis
NMNAT
-
 Leishmania braziliensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Leishmania braziliensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.718
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method Leishmania braziliensis
0.73
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method Leishmania braziliensis
0.76
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method Leishmania braziliensis
0.969
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method Leishmania braziliensis
0.984
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method Leishmania braziliensis
1.174
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method Leishmania braziliensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Leishmania braziliensis

General Information

General Information Comment Organism
additional information structural homology modeling using human NMNAT3, PDB ID 1NUP, B chain, as a template, overview Leishmania braziliensis
physiological function nicotinamide mononucleotide adenylyltransferase catalyzes the central step in nicotinamide adenine dinucleotide (NAD+) biosynthesis, making it essential for survival Leishmania braziliensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.771
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method Leishmania braziliensis
0.789
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method Leishmania braziliensis
0.951
-
 nicotinamide ribonucleotide pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method Leishmania braziliensis
6.218
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method Leishmania braziliensis
6.549
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method Leishmania braziliensis
7.481
-
 ATP pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method Leishmania braziliensis