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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

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.1 Phosphotransferases with an alcohol group as acceptor
                2.7.1.23 NAD+ kinase

Engineering

Engineering on EC 2.7.1.23 - NAD+ kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P117S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S/P117S
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
S57P
-
the variation is associated with the decreased enzyme activity
P117S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S/P117S
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
-
S57P
-
the variation is associated with the decreased enzyme activity
-
P117S
Corynebacterium glutamicum subsp. lactofermentum
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S
Corynebacterium glutamicum subsp. lactofermentum
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
P57S/P117S
Corynebacterium glutamicum subsp. lactofermentum
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
S57P
Corynebacterium glutamicum subsp. lactofermentum
-
the variation is associated with the decreased enzyme activity
P117S
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the mutation results in increased ATP-NAD+ kinase activity and ATP-NADH kinase activity
-
P57S/P117S
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the double mutation only exhibits a little higher activity than P117S-single point mutation. The catalytic efficiency of the mutant improves greatly, which is 6.8 (for NAD+) and 3.2fold (for ATP) higher than that of the wild type enzyme
-
S57P
Corynebacterium glutamicum subsp. lactofermentum JHI3-156
-
the variation is associated with the decreased enzyme activity
-
R175E
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175G
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175H
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175I
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175K
-
no conversion of NAD+ kinase activity to NADH kinase activity
R175Q
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
R175T
-
shows both ATP-dependent NAD+ kinase activity and NADH kinase activity
D45N
-
only minor changes, its active site is similar to that of the wild-type enzyme with the ligand present in the same conformation. The asparagine adopts the same buried conformation as the aspartate but does not form any hydrogen bond with NAD. Mutation results in a 10fold decrease in activity
H223E
-
is twice less active than the wild-type on the biologically relevant substrate NAD. In contrast, its activity toward di-(5'-thioadenosine) is increased 2fold
G183R
-
decrease both in NAD+ kinase and NADH kinase activity
G190A
-
no enzymic activity
G198A
-
no enzymic activity
G207A
-
no enzymic activity
G208A
-
decrease in Vmax-value
L192A
-
no enzymic activity
P196A
-
no enzymic activity
S199A
-
decrease in Vmax-value
T195A
-
kinetic parameters similar to wild-type
T197A
-
no enzymic activity
T200A
-
no enzymic activity
Y202A
-
no enzymic activity
additional information