Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Pfoh, R.; Pai, E.F.; Saridakis, V.
    Nicotinamide mononucleotide adenylyltransferase displays alternate binding modes for nicotinamide nucleotides (2015), Acta Crystallogr. Sect. D, 71, 2032-2039.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.1 gene MTH_150, recombinant overexpression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Gold (DE3) Methanothermobacter thermautotrophicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.1 purified detagged recombinant wild-type and mutant enzymes, hanging drop vapour diffusion, method screening, mixing of 0.002 ml of 10 mg/ml protein in 10 mM HEPES, pH 7.5, 0.5 M NaCl, and 5 mM ligand NAD+ or NADP+, with 0.002 ml of reservoir solution containing 1.5-1.6 M ammonium sulfate, 5% glycerol, 100 mM Tris, pH 8.0, and equilibration against 0.5 ml of reservoir solution, 20°C, 48-72 h, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution, molecular replacement Methanothermobacter thermautotrophicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.1 R11K site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex, the mutant shows similar activity and kinetics compared to the wild-type enzyme Methanothermobacter thermautotrophicus
2.7.7.1 R136K site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex, the mutant shows similar activity and kinetics compared to the wild-type enzyme Methanothermobacter thermautotrophicus
2.7.7.1 R47E site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex Methanothermobacter thermautotrophicus
2.7.7.1 R47K site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex Methanothermobacter thermautotrophicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.1 Mg2+ required Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.1 ATP + nicotinamide ribonucleotide Methanothermobacter thermautotrophicus
-
 diphosphate + NAD+
-
 r
2.7.7.1 ATP + nicotinamide ribonucleotide Methanothermobacter thermautotrophicus ATCC 29096
-
 diphosphate + NAD+
-
 r
2.7.7.1 additional information Methanothermobacter thermautotrophicus bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP ?
-
 ?
2.7.7.1 additional information Methanothermobacter thermautotrophicus ATCC 29096 bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.1 Methanothermobacter thermautotrophicus O26253 gene MTH_150
-
2.7.7.1 Methanothermobacter thermautotrophicus ATCC 29096 O26253 gene MTH_150
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.1 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 Gold (DE3) by anion exchange and nickel affinity chromatography, tag cleavage by thrombin, dialysis, and ultrafiltration Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.1 ATP + nicotinamide ribonucleotide
-
 Methanothermobacter thermautotrophicus diphosphate + NAD+
-
 r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
 Methanothermobacter thermautotrophicus ATCC 29096 diphosphate + NAD+
-
 r
2.7.7.1 additional information bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP Methanothermobacter thermautotrophicus ?
-
 ?
2.7.7.1 additional information the wild-type enzyme traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the enzyme complex. Binding structure of wild-type and mutant enzymes with NAD+ and NADP+, detailed overview Methanothermobacter thermautotrophicus ?
-
 ?
2.7.7.1 additional information bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP Methanothermobacter thermautotrophicus ATCC 29096 ?
-
 ?
2.7.7.1 additional information the wild-type enzyme traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the enzyme complex. Binding structure of wild-type and mutant enzymes with NAD+ and NADP+, detailed overview Methanothermobacter thermautotrophicus ATCC 29096 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.1 nicotinamide mononucleotide adenylyltransferase
-
 Methanothermobacter thermautotrophicus
2.7.7.1 NMNAT
-
 Methanothermobacter thermautotrophicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.1 65
-
 assay at Methanothermobacter thermautotrophicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.1 7.5
-
 assay at Methanothermobacter thermautotrophicus

General Information

EC Number General Information Comment Organism
2.7.7.1 metabolism nicotinamide mononucleotide adenylyltransferase (NMNAT) catalyzes the biosynthesis of NAD+ and NaAD+ Methanothermobacter thermautotrophicus
2.7.7.1 additional information residues Arg11 and Arg136 are implicated in binding the phosphate groups of the ATP substrate. Residue Arg47 does not interact with either NMN or ATP substrates directly, but is deemed to play a role in binding as it is proximal to Arg11 and Arg136, plasticity of the active site Methanothermobacter thermautotrophicus