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Literature summary extracted from

  • O'Hara, J.K.; Kerwin, L.J.; Cobbold, S.A.; Tai, J.; Bedell, T.A.; Reider, P.J.; Llinas, M.
    Targeting NAD+ metabolism in the human malaria parasite Plasmodium falciparum (2014), PLoS ONE, 9, e94061.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.18 gene PF13_0159, phylogenetic tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 (RIL Codon PLUS), recombinant expression of GFP-tagged enzyme in Plasmodium falciparum ring stage D10 culture cells Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.18 D110A site-directed mutagenesis replacing the conserved catalytic site, inactive mutant Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.18 5-(4-bromophenyl)-N'-[(E)-(1-methyl-1H-indol-3-yl)methylidene]-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 5-(4-bromophenyl)-N'-[(E)-(2,3-dimethoxynaphthalen-1-yl)methylidene]-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 5-(4-fluorophenyl)-N'-[(E)-(1-methyl-1H-indol-3-yl)methylidene]-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 5-[(2E)-2-(anthracen-9-ylmethylidene)hydrazinyl]-N-(4-bromophenyl)-5-oxopentanamide
-
 Plasmodium falciparum
2.7.7.18 5-[(2E)-2-(anthracen-9-ylmethylidene)hydrazinyl]-N-(4-fluorophenyl)-5-oxopentanamide
-
 Plasmodium falciparum
2.7.7.18 5-[(2E)-2-(biphenyl-4-ylmethylidene)hydrazinyl]-N-(4-bromophenyl)-5-oxopentanamide
-
 Plasmodium falciparum
2.7.7.18 5-[(2E)-2-(biphenyl-4-ylmethylidene)hydrazinyl]-N-(4-fluorophenyl)-5-oxopentanamide
-
 Plasmodium falciparum
2.7.7.18 5-[(2E)-2-[(2,3-dimethoxynaphthalen-1-yl)methylidene]hydrazinyl]-N-(4-fluorophenyl)-5-oxopentanamide
-
 Plasmodium falciparum
2.7.7.18 5-[(4-bromophenyl)amino]-N'-[(E)-(1-methyl-1H-indol-3-yl)methylidene]hex-5-enehydrazide
-
 Plasmodium falciparum
2.7.7.18 additional information inhibitor synthesis and in vivo evaluation, MIC50 values determined using a standard SYBR green growth assay on synchronous ring stage parasites, overview Plasmodium falciparum
2.7.7.18 N'-[(E)-(2,3-dimethoxynaphthalen-1-yl)methylidene]-5-(4-fluorophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(2-bromophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(2-hydroxyphenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(3-bromophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(3-hydroxyphenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(4-bromophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(4-fluorophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-anthracen-9-ylmethylidene]-5-(4-hydroxyphenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-biphenyl-4-ylmethylidene]-5-(4-bromophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N'-[(E)-biphenyl-4-ylmethylidene]-5-(4-fluorophenyl)-4-oxopentanehydrazide
-
 Plasmodium falciparum
2.7.7.18 N-(4-bromophenyl)-5-[(2E)-2-[(2,3-dimethoxynaphthalen-1-yl)methylidene]hydrazinyl]-5-oxopentanamide
-
 Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.18 0.0199
-
 ATP recombinant His6-tagged enzyme, pH 7.5, 37°C Plasmodium falciparum
2.7.7.18 0.0358
-
 nicotinate beta-D-ribonucleotide recombinant His6-tagged enzyme, pH 7.5, 37°C Plasmodium falciparum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.7.18 cytoplasm
-
 Plasmodium falciparum 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.18 Mg2+ required Plasmodium falciparum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.18 26000
-
-
 Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.18 ATP + nicotinate beta-D-ribonucleotide Plasmodium falciparum
-
 diphosphate + deamido-NAD+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.18 Plasmodium falciparum Q8IE38 3D7 and D10 clones, gene PF13_0159
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.18 recombinant His6-tagged enzyme from Escherichia coli strain BL21 (RIL Codon PLUS) by nickel affinity chromatography Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.18 ATP + nicotinate beta-D-ribonucleotide
-
 Plasmodium falciparum diphosphate + deamido-NAD+
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.18 ? x * 26000, recombinant His6-tagged enzyme, SDS-PAGE Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.7.7.18 nicotinate mononucleotide adenylyltransferase
-
 Plasmodium falciparum
2.7.7.18 PfNMNAT
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.18 37
-
 assay at Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.18 7.5
-
 assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.18 ATP
-
 Plasmodium falciparum

General Information

EC Number General Information Comment Organism
2.7.7.18 evolution the enzyme is highly diverged from the human homologue, but genetically similar to bacterial NMNATs Plasmodium falciparum
2.7.7.18 metabolism the essential enzyme catalyzes one step in the NAD+ pathway that synthesizes NAD+ from exogenous niacin Plasmodium falciparum
2.7.7.18 additional information residue Asp110 is thought to either hydrogen bond with the adenosine monophosphate during the adenylyltransferase reaction or help with essential Mg+2 coordination during catalysis, the residue has an essential function Plasmodium falciparum
2.7.7.18 physiological function the enzyme is essential for NAD+ metabolism. The enzyme is able to genetically complement the closely related Escherichia coli NMNAT enzyme Plasmodium falciparum