Hinolinat sintaza

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Hinolinat sintaza
Identifikatori
EC broj 2.5.1.72
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Hinolinat sintaza (EC 2.5.1.72, NadA, QS, hinolinatna sintetaza) je enzim sa sistematskim imenom gliceron fosfat:iminosukcinatna alkiltransferaza (ciklizacija).[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

gliceron fosfat + iminozukcinat piridin-2,3-dikarboksilat + 2H2O + fosfat

Ovah gvožđe-sumporni protein sadrži [4Fe-4S] klaster.

Reference[uredi | uredi kod]

  1. Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. (2005). „Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis”. FEBS Lett. 579: 3737-3743. PMID 15967443. 
  2. Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. (2006). „Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid”. Plant Physiol. 141: 851-857. PMID 16698895. 
  3. Sakuraba, H., Tsuge, H., Yoneda, K., Katunuma, N. and Ohshima, T. (2005). „Crystal structure of the NAD biosynthetic enzyme quinolinate synthase”. J. Biol. Chem. 280: 26645-26648. PMID 15937336. 
  4. Rousset, C., Fontecave, M. and Ollagnier de Choudens, S. (2008). „The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: Investigation of cluster ligands”. FEBS Lett. 582: 2937-2944. PMID 18674537. 
  5. Saunders, A.H. and Booker, S.J. (2008). „Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation”. Biochemistry 47: 8467-8469. PMID 18651751. 

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