Literature summary for 2.7.1.22 extracted from

Singh, S.K.; Kurnasov, O.V.; Chen, B.; Robinson, H.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenyltransferase and ribosylnicotinimide kinase activities (2002), J. Biol. Chem., 277, 33291-33299.

Search for more literature for 2.7.1.22

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion, 10 mg/ml protein in 100 mM Hepes, pH 7.2, 300 mM NaCl, 1 mM dithiothreitol are incubated with 3 mM NAD and 3 mM ATP and mixed with an equal volume of the reservoir solution consisting of 100 mM MES, pH 6.0, 1 M ammonium sulfate, crystal structure of enzyme complexed with NAD	Haemophilus influenzae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
150000	-	at 0.4 mg/ml protein, analytical ultracentrifugation	Haemophilus influenzae
170000	-	at 1.2 mg/ml protein, analytical ultracentrifugation	Haemophilus influenzae
180000	-	deduced from nucleotide sequence	Haemophilus influenzae

Organism

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme, Ni2+-nitrilotriacetic acid-agarose, Superdex 200	Haemophilus influenzae

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + N-ribosylnicotinamide	-	Haemophilus influenzae	ADP + nicotinamide ribonucleotide	-	?

Subunits

Subunits	Comment	Organism
tetramer	-	Haemophilus influenzae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)