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Information on EC 6.3.4.21 - nicotinate phosphoribosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39683

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     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.21 nicotinate phosphoribosyltransferase
IUBMB Comments
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 .
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Saccharomyces cerevisiae
UNIPROT: P39683
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
nicotinic acid phosphoribosyltransferase, nicotinate phosphoribosyltransferase, naprtase, naprt1, na phosphoribosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nicotinic acid phosphoribosyltransferase
-
niacin ribonucleotidase
-
-
-
-
nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase
-
-
-
-
nicotinic acid mononucleotide glycohydrolase
-
-
-
-
additional information
enzyme is a member of the phosphoribosyltransferase superfamily or PRTase superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
active site structure
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming)
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-26-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
essential for the NAD salvage pathway
-
-
r
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
1 mol ATP is hydrolyzed to ADP plus phosphate per mol product formed
CTP
-
one third the activity of ATP
GTP
-
shows almost as much activity as ATP
ITP
-
shows almost as much activity as ATP
UTP
-
one third the activity of ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phospho-alpha-D-ribose 1-diphosphate
ATP
-
at high concentrations with Mg2+ below 0.03 mM
Mg2+
-
above 10 mM, significant pH alterations
MgADP-
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non-competitive to Mg-ATP or Mg-diphosphate
nicotinate mononucleotide
phosphate
-
0.1 M and above
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
functional modulation by ATP via autophosphorylation of His232, activation by ATP hydrolysis, determination of the binding site
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.07 - 0.09
ATP
0.023
nicotinate
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
broad
additional information
-
pI: 6.9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
-
about half-maximal activity at pH 5.5 and 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
gel filtration
45000
-
SDS-PAGE in the presence and absence of mercaptoethanol
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant selenomethionine-labeled enzyme, 10-30 mg/ml, in 10 mM Tris, pH 7.8, 150 mM NaCl, nanodroplet vapour diffusion method, 4°C, reservoir solution contains 6-16% PEG 5000 monomethyl ether, 0.06 M MES, and 0.04 M NaMES, pH 6.0, usage of 15-20% ethylene glycol as cryoprotectant, X-ray structure determination and analysis at 1.75 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
5 min: 95% loss of activity, MgATP2-, Mg-phosphoribose diphosphate, ATP, GTP or nicotinic acid protect, with 27%, 37%, 52%, 54% or 61% loss of activity, respectively. 10 min: 97% loss of activity, MgATP2-, Mg-5-phospho-alpha-D-ribose 1-diphosphate, ATP, GTP or nicotinic acid protect, with 43%, 52%, 60%, 63% or 69% loss of activity, respectively
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heat, unstable to, substrates protect
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-25°C, at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally tagged selenomethionine-labeled enzyme variant from Escherichia coli strain DL41
extraction, ammonium sulfate fractionation, chromatography on DEAE-cellulose and hydroxylapatite, 1000fold purified
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extraction, fractionation chromatography on phosphocellulose, hydroxyapatite, blue Sephadex and DEAE-cellulose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-terminally tagged enzyme as selenomethionine-labeled variant in Escherichia coli strain DL41
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kosaka, A.; Spivey, H.O.; Gholson, R.K.
Nicotinate phosphoribosyltransferase of yeast. Purification and properties
J. Biol. Chem.
246
3277-3283
1971
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hanna, L.S.; Hess, S.L.; Sloan, D.L.
Kinetic analysis of nicotinate phosphoribosyltransferase from yeast using high pressure liquid chromatography
J. Biol. Chem.
258
9745-9754
1983
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kosaka, A.; Spivey, H.O.; Gholson, R.K.
Yeast nicotinic acid phosphoribosyltransferase. Studies of reaction paths, phosphoenzyme, and Mg2+ effects
Arch. Biochem. Biophys.
179
334-341
1977
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Rajavel, M.; Lalo, D.; Gross, J.W.; Grubmeyer, C.
Conversion of a cosubstrate to an inhibitor. Phosphorylation mutants of nicotinic acid phosphoribosyltransferase
Biochemistry
37
4181-4188
1998
Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae (P39683), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Grubmeyer, C.T.; Gross, J.W.; Rajavel, M.
Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase
Methods Enzymol.
308
28-48
1999
Mycobacterium tuberculosis (P9WJW5), Mycobacterium tuberculosis H37Rv (P9WJW5), Saccharomyces cerevisiae, Saccharomyces cerevisiae (P39683), Salmonella enterica subsp. enterica serovar Typhimurium (P22253)
Manually annotated by BRENDA team
Chappie, J.S.; Canaves, J.M.; Han, G.W.; Rife, C.L.; Xu, Q.; Stevens, R.C.
The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases
Structure
13
1385-1396
2005
Saccharomyces cerevisiae (P39683), Saccharomyces cerevisiae
Manually annotated by BRENDA team