Enzyme

Download
EC Tree
     2. Transferases
        2.4 Glycosyltransferases
            2.4.2 Pentosyltransferases
ID:2.4.2.19
Description:Nicotinate-nucleotide diphosphorylase (carboxylating).
Alternative Name: Quinolinate phosphoribosyltransferase (decarboxylating).
Nicotinate-nucleotide pyrophosphorylase (carboxylating).
Cath: 3.20.20.70; 3.90.1170.20; 3.40.50.10800;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.2.19
BRENDA Enzyme Link: BRENDA 2.4.2.19
KEGG Enzyme Link: KEGG2.4.2.19
BioCyc Enzyme Link: BioCyc 2.4.2.19
ExPASy Enzyme Link: ExPASy2.4.2.19
EC2PDB Enzyme Link: EC2PDB 2.4.2.19
ExplorEnz Enzyme Link: ExplorEnz 2.4.2.19
PRIAM enzyme-specific profiles Link: PRIAM 2.4.2.19
IntEnz Enzyme Link: IntEnz 2.4.2.19
MEDLINE Enzyme Link: MEDLINE 2.4.2.19
MSA:

2.4.2.19;

Phylogenetic Tree:

2.4.2.19;

Uniprot:
M-CSA:
RHEA:12733 CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n+;H0:4](:[*:5]):[cH;+0:6]:[*:7].[*:8]-[OH;+0:9].[*:10]=[C;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:9]-[*:8].[*:10]=[C;H0;+0:11](-[OH;+0:12])-[c;H0;+0:6](:[*:7]):[n;H0;+0:4]:[*:5]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from homo sapiens.Liu H, Woznica K, Catton G, Crawford A, Botting N, Naismith JH2007 Oct 2617868694
Crystal structure of quinolinic acid phosphoribosyltransferase from Helicobacter pylori.Kim MK, Im YJ, Lee JH, Eom SH2006 Apr 116419067
Quinolinate phosphoribosyltransferase: kinetic mechanism for a type II PRTase.Cao H, Pietrak BL, Grubmeyer C2002 Mar 1211876660