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Information on EC 6.3.1.5 - NAD+ synthase and Organism(s) Bacillus anthracis and UniProt Accession Q81RP3

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.1 Acid—ammonia (or amine) ligases (amide synthases)
                6.3.1.5 NAD+ synthase
IUBMB Comments
L-Glutamine also acts, more slowly, as amido-donor [cf. EC 6.3.5.1].
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This record set is specific for:
Bacillus anthracis
UNIPROT: Q81RP3
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The taxonomic range for the selected organisms is: Bacillus anthracis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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ATP
+
deamido-NAD+
+
NH3
=
AMP
+
diphosphate
+
NAD+
+
+
=
+
+
Synonyms
nads, nad synthetase, nad+ synthetase, nad synthase, nicotinamide adenine dinucleotide synthetase, nad+ synthase, nh3-dependent nad+ synthetase, ammonia-specific nad synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD+ synthetase
-
Diphosphopyridine nucleotide synthetase
-
-
-
-
NAD synthetase
-
-
-
-
NAD+ synthetase
-
-
-
-
Nicotinamide adenine dinucleotide synthetase
-
-
-
-
Synthetase, nicotinamide adenine dinucleotide
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
deamido-NAD+:ammonia ligase (AMP-forming)
L-Glutamine also acts, more slowly, as amido-donor [cf. EC 6.3.5.1].
CAS REGISTRY NUMBER
COMMENTARY hide
9032-69-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.289
ATP
in 60 mM EPPS pH 8.5 with 20 mM ammonium chloride, 20 mM potassium chloride, and 10 mM magnesium chloride, at 37°C
0.152
deamido-NAD+
in 60 mM EPPS pH 8.5 with 20 mM ammonium chloride, 20 mM potassium chloride, and 10 mM magnesium chloride, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NADE_BACAN
272
0
30101
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method using 8-12% PEG 8000, 0.505 M ammonium sulfate, 6% glycerol, 100 mM magnesium chloride, 0.05% n-octyl-beta-D-glucopyranoside, 100 mM HEPES, pH 7
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni HiTrap column chromatography, and Superdex-200 gel filtration or Superdex-75 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McDonald, H.M.; Pruett, P.S.; Deivanayagam, C.; Protasevich, I.I.; Carson, W.M.; DeLucas, L.J.; Brouillette, W.J.; Brouillette, C.G.
Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis
Acta Crystallogr. Sect. D
63
891-905
2007
Bacillus anthracis (Q81RP3), Bacillus anthracis
Manually annotated by BRENDA team