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Literature summary for 2.5.1.72 extracted from

  • Volbeda, A.; Darnault, C.; Renoux, O.; Reichmann, D.; Amara, P.; Ollagnier de Choudens, S.; Fontecilla-Camps, J.C.
    Crystal Structures of quinolinate synthase in complex with a substrate analogue, the condensation intermediate, and substrate-derived product (2016), J. Am. Chem. Soc., 138, 11802-11809 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant K219R/Y107F in complex with the first intermediate resulting from the condensation of dihydroxyacetone phosphate with iminoaspartate and the dihydroxyacetone phosphate analogue phosphoglycolohydroxamate, and mutant K219R/Y21F in complex with quinolinic acid. Phosphoglycolohydroxamate binds to NadA with its phosphate group at the site where the carboxylate groups of the first intermediate also bind Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
K219R mutant is able to bind citrate Thermotoga maritima
K219R/Y107F crystallization data. The mutated protein is unable to catalyze the aldo-keto isomerization and/or cyclization of the first intermediate resulting from the condensation of dihydroxyacetone phosphate with iminoaspartate that ultimately leads to quinolinic acid formation Thermotoga maritima
K219R/Y21F crystallization data Thermotoga maritima
Y21F mutant is able to bind citrate Thermotoga maritima

Organism

Organism UniProt Comment Textmining
Thermotoga maritima Q9X1X7
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Thermotoga maritima DSM 3109 Q9X1X7
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Synonyms

Synonyms Comment Organism
NadA
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Thermotoga maritima