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Literature summary for extracted from

  • Ruszkowski, M.; Dauter, Z.
    Structures of Medicago truncatula L-histidinol dehydrogenase show rearrangements required for NAD+ binding and the cofactor positioned to accept a hydride (2017), Sci. Rep., 7, 10476 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structures in complex with imidazole, histidinol, and His with NAD+ Medicago truncatula


Localization Comment Organism GeneOntology No. Textmining
Medicago truncatula 9507


Organism UniProt Comment Textmining
Medicago truncatula G7IKX3


Synonyms Comment Organism
Medicago truncatula

General Information

General Information Comment Organism
metabolism reaction mechanism: a proton is withdrawn from the histidinol O atom by Nepsilon of His368 (Base 1) that becomes double-protonated, and one hydride is abstracted by the first NAD+ molecule, and histidinaldehyde is formed. The used NADH dissociates and is replaced by the second NAD+ molecule. A water molecule is activated by Glu367 (Base 2) and performs a nucleophilic attack on the reactive carbon, forming a new C-O bond. Simultaneously, the histidinaldehyde oxygen withdraws the proton back from Nepsilon of His368, resulting in the formation of a gem-diol histidinaldehyde hydrate. In the next step, His368 abstracts a proton from one of the hydroxyl groups of histidinaldehyde hydrate, whereas the second NAD+ removes hydride from the reactive carbon, producing His Medicago truncatula