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Information on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase and Organism(s) Bacillus anthracis and UniProt Accession C3L5T6

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Bacillus anthracis
UNIPROT: C3L5T6 not found.
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The taxonomic range for the selected organisms is: Bacillus anthracis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nicotinate mononucleotide adenylyltransferase, nicotinic acid mononucleotide adenylyltransferase, pfnmnat, namn at, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylyltransferase, nicotinate mononucleotide
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-
-
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deamido-NAD+ pyrophosphorylase
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-
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deamidonicotinamide adenine dinucleotide pyrophosphorylase
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NaMN AT
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NaMN-ATase
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nicotinamide/nicotinic acid mononucleotide adenylyltransferase
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nicotinic acid mononucleotide adenylyltransferase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinate-ribonucleotide adenylyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-98-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
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-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
NaMNAT is the penultimate enzyme in the biosynthesis of NAD+ and catalyzes the adenylation of nicotinic acid mononucleotide by ATP to form nicotinic acid adenine dinucleotide
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide]
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4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide
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[(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.044
ATP
pH 7.5, recombinant enzyme
0.025
nicotinate ribonucleotide
pH 7.5, recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide]
Bacillus anthracis
pH 7.5, 22°C
0.025
4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide
Bacillus anthracis
pH 7.5, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
probable
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23347
x * 23347, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 23347, sequence calculation
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors 4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide, 4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide], and [(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid. 4-[2-(Anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide binds at an enzyme monomer-monomer interface formed in the crystal of the complex, it sits at a central cleft between strands beta1 and beta4 of the beta sheet, which is the catalytic and substrate binding sites of the enzyme. The structures reveal a common binding site near residues Trp117, Try112, and Met109. This site overlaps but is distinct from the substrate-binding pocket
sitting drop and hanging drop vapour diffusion method, mixing 0.001 ml of 4 mg/ml protein in 50 mM Tris, pH 7.0, 100 mM NaCl, 100 mM Arg, 100 mM Glu, 1% glycerol, 1 mM DTT, and containing 200 mM trehalose, with 0.001 ml of reservoir solution containing 2.1 M ammonium sulfate, 100 mM HEPES pH 7.0, 2% PEG 400 and 10 mM MgCl2, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, usage molecular replacement and of self-interaction chromatography for process optimization
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nadD, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is a target for inhibitor development
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lu, S.; Smith, C.D.; Yang, Z.; Pruett, P.S.; Nagy, L.; McCombs, D.; Delucas, L.J.; Brouillette, W.J.; Brouillette, C.G.
Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis
Acta Crystallogr. Sect. F
64
893-898
2008
Bacillus anthracis (A0A6L7H177), Bacillus anthracis
Manually annotated by BRENDA team
Zhai, R.G.; Rizzi, M.; Garavaglia, S.
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme
Cell. Mol. Life Sci.
66
2805-2818
2009
Bacillus anthracis, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Huang, N.; Kolhatkar, R.; Eyobo, Y.; Sorci, L.; Rodionova, I.; Osterman, A.L.; Mackerell, A.D.; Zhang, H.
Complexes of bacterial nicotinate mononucleotide adenylyltransferase with inhibitors: implication for structure-based drug design and improvement
J. Med. Chem.
53
5229-5239
2010
Bacillus anthracis (C3L5T6), Bacillus anthracis, Bacillus anthracis CDC 684 (C3L5T6)
Manually annotated by BRENDA team