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PDBsum entry 6f4l
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References listed in PDB file
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Key reference
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Title
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Crystallographic trapping of reaction intermediates in quinolinic acid synthesis by nada.
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Authors
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A.Volbeda,
J.Saez cabodevilla,
C.Darnault,
O.Gigarel,
T.H.Han,
O.Renoux,
O.Hamelin,
S.Ollagnier-De-Choudens,
P.Amara,
J.C.Fontecilla-Camps.
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Ref.
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ACS Chem Biol, 2018,
13,
1209-1217.
[DOI no: ]
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PubMed id
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Abstract
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NadA is a multifunctional enzyme that condenses dihydroxyacetone phosphate
(DHAP) with iminoaspartate (IA) to generate quinolinic acid (QA), the universal
precursor of the nicotinamide adenine dinucleotide (NAD(P)) cofactor. Using
X-ray crystallography, we have (i) characterized two of the reaction
intermediates of QA synthesis using a "pH-shift" approach and a slowly
reacting Thermotoga maritima NadA variant and (ii) observed the QA product,
resulting from the degradation of an intermediate analogue, bound close to the
entrance of a long tunnel leading to the solvent medium. We have also used
molecular docking to propose a condensation mechanism between DHAP and IA based
on two previously published Pyrococcus horikoshi NadA structures. The
combination of reported data and our new results provide a structure-based
complete catalytic sequence of QA synthesis by NadA.
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Secondary reference #1
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Title
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Crystal structures of quinolinate synthase in complex with a substrate analogue, The condensation intermediate, And substrate-Derived product.
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Authors
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A.Volbeda,
C.Darnault,
O.Renoux,
D.Reichmann,
P.Amara,
S.Ollagnier de choudens,
J.C.Fontecilla-Camps.
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Ref.
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J Am Chem Soc, 2016,
138,
11802-11809.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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The crystal structure of fe₄s₄ quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-Type triad.
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Authors
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M.V.Cherrier,
A.Chan,
C.Darnault,
D.Reichmann,
P.Amara,
S.Ollagnier de choudens,
J.C.Fontecilla-Camps.
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Ref.
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J Am Chem Soc, 2014,
136,
5253-5256.
[DOI no: ]
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PubMed id
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