Any feedback?
Please rate this page

BRENDA support

Literature summary for extracted from

  • Shin, D.H.; Oganesyan, N.; Jancarik, J.; Yokota, H.; Kim, R.; Kim, S.H.
    Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum (2005), J. Biol. Chem., 280, 18326-18335.
    View publication on PubMed


Cloned (Comment) Organism
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 Thermoplasma acidophilum

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Thermoplasma acidophilum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6 * 43000, (alphabeta)3, SDS-PAGE and crystal structure analysis Thermoplasma acidophilum


Organism UniProt Comment Textmining
Thermoplasma acidophilum Q9HJ28

Purification (Commentary)

Purification (Comment) Organism
recombinant tagged wild-type and selenomethionine-labeled fusion enzymes from Escherichia coli to homogeneity by high-trap chelating nickel affinity chromatography Thermoplasma acidophilum


Reaction Comment Organism Reaction ID
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate active site structure Thermoplasma acidophilum


Subunits Comment Organism
hexamer 6 * 43000, (alphabeta)3, SDS-PAGE and crystal structure analysis Thermoplasma acidophilum
More enzyme monomer consists of 3 dimeric domains: an N-terminal alpha + beta domain, a central alpha/beta domain, and a C-terminal domain containing an unique zinc finger Thermoplasma acidophilum


Synonyms Comment Organism
Thermoplasma acidophilum