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Literature summary for 1.1.1.23 extracted from
- 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 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structures in complex with imidazole, histidinol, and His with NAD+ | Medicago truncatula |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | - |
Medicago truncatula | 9507 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Medicago truncatula | G7IKX3 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 11412251 | - |
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| metabolism | reaction mechanism: a proton is withdrawn from the histidinol O atom by Nepsilon of His368 (Base 1) that becomes double-protonated, and one hydride is abstracted by the first NAD+ molecule, and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 |
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Release 2023.1 (January 2023)
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