Structural basis for the stereospecific inhibition of the dual proline/hydroxyproline catabolic enzyme ALDH4A1 by trans‐4‐hydroxy‐L‐proline

Aldehyde dehydrogenase 4A1 (ALDH4A1) catalyzes the final steps of both proline and hydroxyproline catabolism. It is a dual substrate enzyme that catalyzes the NAD+‐dependent oxidations of L‐glutamate‐γ‐semialdehyde to L‐glutamate (proline metabolism), and 4‐hydroxy‐L‐glutamate‐γ‐semialdehyde to 4‐er...

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Veröffentlicht in:	Protein science 2021-08, Vol.30 (8), p.1714-1722
Hauptverfasser:	Bogner, Alexandra N., Stiers, Kyle M., McKay, Cole M., Becker, Donald F., Tanner, John J.
Format:	Artikel
Sprache:	eng
Schlagworte:	1-Pyrroline-5-Carboxylate Dehydrogenase - antagonists & inhibitors 1-Pyrroline-5-Carboxylate Dehydrogenase - chemistry 1-Pyrroline-5-Carboxylate Dehydrogenase - metabolism Aldehyde dehydrogenase Aldehydes ALDH4A1 Animals Catabolism Crystal structure Crystallography Crystallography, X-Ray Drug delivery enzyme inhibition Enzymes Full‐Length Paper Full‐Length Papers Hydrogen bonding Hydrogen bonds Hydroxyproline Hydroxyproline - chemistry hydroxyproline catabolism L‐glutamate‐γ‐semialdehyde dehydrogenase Metabolism Mice Models, Molecular NAD Proline Proline - chemistry proline metabolism Pyrrolidine Selectivity Serine Stereoisomerism Stereoisomers Substrate inhibition X‐ray crystallography
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