Reference on EC 2.5.1.72 - quinolinate synthase and Organism(s) Pyrococcus horikoshii and UniProt Accession O57767
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AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saunders, A.H.; Griffiths, A.E.; Lee, K.H.; Cicchillo, R.M.; Tu, L.; Stromberg, J.A.; Krebs, C.; Booker, S.J.
Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes
Biochemistry
47
10999-11012
2008
Escherichia coli, Mycobacterium tuberculosis, Pyrococcus horikoshii
Sakuraba, H.; Tsuge, H.; Yoneda, K.; Katunuma, N.; Ohshima, T.
Crystal structure of the NAD biosynthetic enzyme quinolinate synthase
J. Biol. Chem.
280
26645-26648
2005
Pyrococcus horikoshii (O57767), Pyrococcus horikoshii
Esakova, O.A.; Silakov, A.; Grove, T.L.; Saunders, A.H.; McLaughlin, M.I.; Yennawar, N.H.; Booker, S.J.
Structure of quinolinate synthase from Pyrococcus horikoshii in the presence of its product, quinolinic acid
J. Am. Chem. Soc.
138
7224-7227
2016
Pyrococcus horikoshii
Fenwick, M.K.; Ealick, S.E.
Crystal structures of the iron-sulfur cluster-dependent quinolinate synthase in complex with dihydroxyacetone phosphate, iminoaspartate analogues, and quinolinate
Biochemistry
55
4135-4139
2016
Pyrococcus horikoshii (O57767), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O57767)
