Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Mycobacterium tuberculosis and UniProt Accession P9WHV7

for references in articles please use BRENDA:EC2.7.1.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mycobacterium tuberculosis
UNIPROT: P9WHV7 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Mycobacterium tuberculosis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
ATP
+
NAD+
=
ADP
+
NADP+
+
=
+
Synonyms
nad kinase, nadk, nad+ kinase, nadk2, nad(h) kinase, utr1p, osnadk1, slr0400, sll1415, c5orf33, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
poly(P)/ATP-NAD kinase
-
ATP:NAD 2'-phosphotransferase
-
-
-
-
DPN kinase
-
-
-
-
kinase (phosphorylating), nicotinamide adenine dinucleotide
-
-
-
-
kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
-
NAD kinase
-
-
-
-
NADK
-
-
-
-
nicotinamide adenine dinucleotide kinase
-
-
-
-
Poly(P)/ATP NAD kinase
-
-
-
-
polyphosphate/ATP-NAD kinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + NAD+ = ADP + NADP+
show the reaction diagram
NAD+-binding mode and intersubunit contact
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 2'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-66-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
?
ATP + NADH
ADP + NADPH
show the reaction diagram
low activity
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate + NAD+
(phosphate)n-1 + NADP+
show the reaction diagram
-
-
-
-
?
polyphosphate + NAD+
?
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
0.4 mM, 43% residual activity
NADP+
-
0.4 mM, 22% residual activity
NADPH
-
0.4 mM, 50% residual activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2 - 2.7
ATP
1.2 - 6.5
NAD+
2.2 - 2.7
Polyphosphate
additional information
additional information
-
allosteric enzyme, Hill coefficient for ATP 1.5, for polyphosphate 1.4
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.5
-
substrates ATP, NAD+, mutant G208A, 37°C, pH 8.0
0.7
-
substrates ATP, NAD+, mutant S199A, 37°C, pH 8.0
1.1
-
substrates ATP, NAD+, mutant T195A, 37°C, pH 8.0
1.2
-
substrates ATP, NAD+, wild-type, 37°C, pH 8.0
2.2
-
substrates polyphosphate, NAD+, mutant G208A, 37°C, pH 8.0
2.5
-
substrates polyphosphate, NAD+, mutant S199A, 37°C, pH 8.0
3.5
-
substrates polyphosphate, NAD+, mutant T195A, 37°C, pH 8.0
3.8
-
substrates polyphosphate, NAD+, wild-type, 37°C, pH 8.0
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
82000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
or tetramer, crystallization data
homotetramer
4 x 35000
tetramer
or dimer, crystallization data
dimer
-
or trimer, 2 * 33000, SDS-PAGE
trimer
-
or dimer, 3 * 33000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo form of Ppnk at 2.8 A resolution. Crystals belong to space group C2 (a=140.2, b=69.4, c=106.4 A, and beta=130°). Holo form of Ppnk complexed with NAD+ at 2.6 A resolution. Crystals belong space group to P62 (a=b=110.5 and c=108.9 A). Overall structures of apo-Ppnk and Ppnk-NAD consist of an N-domain (residues 1-138 and 279-283), a C-domain (residues 139-278), and a C-terminal tail (residues 284-307)
in complex with NAD+
recombinant enzyme, crystallization by hanging-drop vapour-diffusion method with polyethylene glycol 4000 as the precipitant
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
mutants of the NAD kinase gene are lethal
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for several weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, S.; Kawai, S.; Mikami, B.; Murata, K.
Crystallization and preliminary X-ray analysis of NAD kinase from Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. D
57
1319-1320
2001
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team
Mori, S.; Yamasaki, M.; Maruyama, Y.; Momma, K.; Kawai, S.; Hashimoto, W.; Mikami, B.; Murata, K.
NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex
Biochem. Biophys. Res. Commun.
327
500-508
2005
Mycobacterium tuberculosis (P9WHV7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHV7)
Manually annotated by BRENDA team
Raffaelli, N.; Finaurini, L.; Mazzola, F.; Pucci, L.; Sorci, L.; Amici, A.; Magni, G.
Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagenesis
Biochemistry
43
7610-7617
2004
Mycobacterium tuberculosis
Manually annotated by BRENDA team
Garavaglia, S.; Raffaelli, N.; Finaurini, L.; Magni, G.; Rizzi, M.
A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis
J. Biol. Chem.
279
40980-40986
2004
Mycobacterium tuberculosis (P9WHV7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHV7)
Manually annotated by BRENDA team
Mori, S.; Yamasaki, M.; Maruyama, Y.; Momma, K.; Kawai, S.; Hashimoto, W.; Mikami, B.; Murata, K.
Crystallographic studies of Mycobacterium tuberculosis polyphosphate/ATP-NAD kinase complexed with NAD
J. Biosci. Bioeng.
98
391-393
2004
Mycobacterium tuberculosis (P9WHV7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHV7)
Manually annotated by BRENDA team
Kawai, S.; Murata, K.
Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
Biosci. Biotechnol. Biochem.
72
919-930
2008
Arabidopsis thaliana, Arabidopsis thaliana (Q500Y9), Arabidopsis thaliana (Q56YN3), Arabidopsis thaliana (Q9C5W3), Archaeoglobus fulgidus, Bacillus subtilis (O31612), Bacillus subtilis (O34934), Candida albicans, Columba livia, Cyberlindnera jadinii, Dictyostelium discoideum, Escherichia coli (P0A7B3), Glycine max, Homo sapiens, Homo sapiens (O95544), Lactuca sativa, Listeria monocytogenes, Methanocaldococcus jannaschii (Q58327), Micrococcus luteus (Q8VUL9), Mycobacterium tuberculosis (P9WHV7), Mycobacterium tuberculosis H37Rv (P9WHV7), Oryza sativa, Pyrococcus horikoshii (O58801), Saccharomyces cerevisiae (C7GKE4), Saccharomyces cerevisiae (P21373), Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae, Salmonella enterica, Schizosaccharomyces pombe, Sorghum sp., Sphingomonas sp. A1 (Q6L7J5), Synechococcus elongatus PCC 6301, Thermotoga maritima, Triticum sp.
Manually annotated by BRENDA team