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Literature summary for 6.3.5.1 extracted from

  • Sorci, L.; Blaby, I.; De Ingeniis, J.; Gerdes, S.; Raffaelli, N.; de Crecy Lagard, V.; Osterman, A.
    Genomics-driven reconstruction of acinetobacter NAD metabolism: insights for antibacterial target selection (2010), J. Biol. Chem., 285, 39490-39499.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.5.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as a His-tagged fusion protein Acinetobacter baumannii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 deamido-NAD+ pH 7.5, 30°C Acinetobacter baumannii
4.3
-
 deamido-NMN pH 7.5, 30°C Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
-
-
-
Acinetobacter baumannii B0V8W9
-
-

Purification (Commentary)

Purification (Comment) Organism
using Ni-NTA chromatography Acinetobacter baumannii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + deamido-NAD+ + L-Gln
-
 Acinetobacter baumannii AMP + diphosphate + NAD+ + L-Glu
-
 ?
ATP + deamido-NAD+ + NH3 + H2O
-
 Acinetobacter baumannii AMP + diphosphate + NAD+
-
 ?
ATP + deamido-NMN + L-Gln poor substrate Acinetobacter baumannii AMP + diphosphate + NMN + L-Glu
-
 ?

Synonyms

Synonyms Comment Organism
abNadE enzyme possesses an additional glutamine transferase domain Acinetobacter baumannii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Acinetobacter baumannii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0032
-
 deamido-NMN pH 7.5, 30°C Acinetobacter baumannii
0.57
-
 deamido-NAD+ pH 7.5, 30°C Acinetobacter baumannii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Acinetobacter baumannii

General Information

General Information Comment Organism
malfunction nadE is dispensable when the nondeamidating salvage pathway functions as the only route of NAD biogenesis Acinetobacter baumannii
metabolism due to the presence of an additional glutamine transferase domain, abNadE can efficiently utilize l-glutamine (as well as ammonia) for the amidation of NAD precursor Acinetobacter baumannii
physiological function nadE, encoding glutamine-dependent NAD synthetase, is dispensable when the nondeamidating salvage pathway of nicotinamide salvage/recycling functions as the only route of NAD biogenesis Acinetobacter baumannii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00074
-
 deamido-NMN pH 7.5, 30°C Acinetobacter baumannii
34
-
 deamido-NAD+ pH 7.5, 30°C Acinetobacter baumannii