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Literature summary 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)

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

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.23 chloroplast
-
 Medicago truncatula 9507
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.23 Medicago truncatula G7IKX3
-
-

Synonyms

EC Number Synonyms Comment Organism
1.1.1.23 11412251
-
 Medicago truncatula

General Information

EC Number General Information Comment Organism
1.1.1.23 metabolism reaction mechanism: a proton is withdrawn from the histidinol O atom by Nepsilon of His368 (Base 1) that becomes double-protonated, and one hydride is abstracted by the first NAD+ molecule, and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