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Literature summary for 2.7.7.1 extracted from

  • Forero-Baena, N.; Sanchez-Lancheros, D.; Buitrago, J.; Bustos, V.; Ramirez-Hernandez, M.
    Identification of a nicotinamide/nicotinate mononucleotide adenylyltransferase in Giardia lamblia (GlNMNAT) (2015), Biochim. Open, 1, 61-69.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.1

Cloned(Commentary)

Cloned (Comment) Organism
genes glnmnat-a and glnmnat-b, encoded on chromosome 3 and 5, respectively, DNA and amino acid sequence determination and analysis, phylogenetic analysis of GlNMNAT isoenzymes, sequence comparisons to human isozymes, recombinant expression of His-tagged glnmnat-a gene product in Escherichia coli strain BL21 Giardia intestinalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics are observed for NMN and ATP, but saturation is not accomplished with NAMN, implying low affinity yet detectable activity with this substrate. Double-reciprocal plots show no cooperativity for this enzyme Giardia intestinalis
1.48 1.52 ATP pH 7.5, 26°C, recombinant isozyme GlNMNAT-A Giardia intestinalis
2.53 2.72 nicotinamide ribonucleotide pH 7.5, 26°C, recombinant isozyme GlNMNAT-A Giardia intestinalis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Giardia intestinalis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25400
-
-
 Giardia intestinalis
28100
-
-
 Giardia intestinalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + nicotinamide ribonucleotide Giardia intestinalis
-
 diphosphate + NAD+
-
 ?
additional information Giardia intestinalis bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Giardia intestinalis A8BIC5 WB clone C6, genes glnmnat-a and glnmnat-b
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography Giardia intestinalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + nicotinamide ribonucleotide
-
 Giardia intestinalis diphosphate + NAD+
-
 ?
additional information bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18 Giardia intestinalis ?
-
 ?

Subunits

Subunits Comment Organism
? x * 25400, about, isozyme GlNMNAT-A, sequence calculation, x * 28100, about, isozyme GlNMNAT-B, sequence calculation Giardia intestinalis
More GlNMNAT tertiary structure model with a Rossmann-type fold, overview Giardia intestinalis

Synonyms

Synonyms Comment Organism
GlNMNAT
-
 Giardia intestinalis
nicotinamide/nicotinate mononucleotide adenylyltransferase
-
 Giardia intestinalis
NMNAT
-
 Giardia intestinalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
26
-
 assay at Giardia intestinalis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.41 2.44 ATP pH 7.5, 26°C, recombinant isozyme GlNMNAT-A Giardia intestinalis
2.97 3.04 nicotinamide ribonucleotide pH 7.5, 26°C, recombinant isozyme GlNMNAT-A Giardia intestinalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Giardia intestinalis

General Information

General Information Comment Organism
metabolism the enzyme is essentially involved in the NAD biosynthesis via two different pathways, overview Giardia intestinalis