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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.4.21 - nicotinate phosphoribosyltransferase and Organism(s) Thermoplasma acidophilum and UniProt Accession Q9HJ28

for references in articles please use BRENDA:EC6.3.4.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermoplasma acidophilum
UNIPROT: Q9HJ28
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Thermoplasma acidophilum
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
niacin ribonucleotidase
-
-
-
-
nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase
-
-
-
-
nicotinic acid mononucleotide glycohydrolase
-
-
-
-
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
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
6 * 43000, (alphabeta)3, SDS-PAGE and crystal structure analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 43000, (alphabeta)3, SDS-PAGE and crystal structure analysis
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant detagged wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, room temperature, 0.001 ml protein solution mixed with equal volume of well solution containing 0.2 M ammonium acetate, 0.1 M Tris-HCl, pH 8.5, 45% 2-methyl-2,4-pentanediol, 1 week, crystallization condition screening using sitting drop vapour diffusion at room temperature, iridium complexed, X-ray diffraction structure determination and analysis at 2.8 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tagged wild-type and selenomethionine-labeled fusion enzymes from Escherichia coli to homogeneity by high-trap chelating nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the enzyme as His6-tagged-maltose-binding fusion protein containing a tobacco etch virus protease cleavage site in Escherichia coli strain BL21(DE3) for the wild-type, and in strain B834(DE3) for a selenomethionine-labeled variant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shin, D.H.; Oganesyan, N.; Jancarik, J.; Yokota, H.; Kim, R.; Kim, S.H.
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum
J. Biol. Chem.
280
18326-18335
2005
Thermoplasma acidophilum (Q9HJ28), Thermoplasma acidophilum
Manually annotated by BRENDA team