2.7.1.23: NAD+ kinase This is an abbreviated version! For detailed information about NAD+ kinase, go to the full flat file .
Reaction
ATP +
NAD+ =
ADP +
NADP+
Synonyms Afnk, AtNADK1, AtNADK2, AtNADK3, ATP: NAD(H) 2'-phosphotransferase, ATP:NAD 2'-phosphotransferase, ATP:NAD+ 2'-phosphotransferase, BsNADK, C5orf33, C5orf33 protein, diphosphopyridine nucleotide kinase, diphosphppyridine kinase, DPN kinase, EC 2.7.1.23, GmNADK1, GmNADK2, GmNADK3, GmNADK4, GmNADK5, HsNADK, kinase (phosphorylating), nicotinamide adenine dinucleotide, kinase, nicotinamide adenine dinucleotide (phosphorylating), MJ0917, NAD kinase, NAD kinase 1, NAD kinase 2, NAD kinase2, NAD(H) kinase, NadF, NADHK, NADK, NADK1, NADK2, NADK3, NADP phosphatase/NAD kinase, native plant calcium- and calmodulin-dependent NAD+-kinase, nicotinamide adenine dinucleotide kinase, OsNADK1, PH1074, Poly(P)/ATP NAD kinase , poly(P)/ATP-NAD kinase, poly(P)/ATPdependent NAD kinase, polyP/ATP-dependent NAD kinase, polyphosphate/ATP-NAD kinase, Pos5, Ppnk, PPNK_THEMA, sll1415, SlNADK1, SlNADK2, slr0040, slr0400, slr1415, SpNADK1, SpNADK2, styNadK, Utr, Utr1, Utr1p, YEF1, Yef1p, YfjB, YjbN, YtdI
ECTree
Subunits
Subunits on EC 2.7.1.23 - NAD+ kinase
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oligomer
-
x * 32000, SDS-PAGE
trimer
-
or dimer, 3 * 33000, SDS-PAGE
additional information
-
Ca2+-dependent calmodulin-binding domain near N-terminal extension of isoform NADK2
?
? x 110000
?
x * 32000, recombinant enzyme, SDS-PAGE
?
x * 29500, calculated from amino acid sequence
?
-
x * 32000, recombinant enzyme, SDS-PAGE
-
?
-
x * 29500, calculated from amino acid sequence
-
?
x * 61269, calculated from sequence
?
-
x * 61269, calculated from sequence
-
?
-
x * 39114, calculation from nucleotide sequence
?
-
x * 31000, SDS-PAGE
-
dimer
or tetramer
dimer
-
2 * 30000, SDS-PAGE
dimer
or tetramer, crystallization data
dimer
-
or trimer, 2 * 33000, SDS-PAGE
dimer
-
or tetramer, crystallization data
-
dimer
-
without effectors, NadK exists as an equilibrium mixture of dimers and tetramers but is converted entirely to tetramers in the presence of the inhibitor NADPH. Comparison of NadK kinetic parameters with pool sizes of NADH and NADPH suggests that NadK is substantially inhibited during normal growth and, thus, can increase its activity greatly in response to temporary drops in the pools of inhibitory NADH and NADPH. The primary inhibitor is NADPH during aerobic growth and NADH during anaerobic growth
dimer
2 * 32000, SDS-PAGE
hexamer
-
6 * 30000, SDS-PAGE
hexamer
-
6 * 30000, SDS-PAGE
-
hexamer
4 * 49228, calculation from nucleotide sequence
homodimer
2 x 38000
homodimer
-
2 * 43000, SDS-PAGE
homodimer
-
2 * 43300, calculated from amino acid sequence
homohexamer
6 x 30000
homohexamer
6 * 60000, Utr1p
homooctamer
8 * 60000
homooctamer
6 * 60000, Yef1p
homotetramer
-
4 * 36000, SDS-PAGE
homotetramer
-
2 * 34300, SDS-PAGE
homotetramer
-
2 * 34300, SDS-PAGE
-
homotetramer
-
4 * 36000, SDS-PAGE
-
homotetramer
Corynebacterium glutamicum subsp. lactofermentum
-
4 * 36000, SDS-PAGE
homotetramer
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
4 * 36000, SDS-PAGE
-
homotetramer
-
4 * 43000, SDS-PAGE
homotetramer
-
crystallography
homotetramer
-
4 x 35000
-
octamer
-
8 * 34000, SDS-PAGE
octamer
-
8 * 60000, SDS-PAGE
tetramer
or dimer
tetramer
or dimer, crystallization data
tetramer
-
or dimer, crystallization data
-
tetramer
4 * 37000, SDS-PAGE
tetramer
-
4 * 31000 SDS-PAGE
tetramer
-
without effectors, NadK exists as an equilibrium mixture of dimers and tetramers but is converted entirely to tetramers in the presence of the inhibitor NADPH. Comparison of NadK kinetic parameters with pool sizes of NADH and NADPH suggests that NadK is substantially inhibited during normal growth and, thus, can increase its activity greatly in response to temporary drops in the pools of inhibitory NADH and NADPH. The primary inhibitor is NADPH during aerobic growth and NADH during anaerobic growth