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Article

The β2αB loop determines NAD(P) cofactor specificity and kinetics in trypanosomal D-3-hydroxybutyrate dehydrogenases.

Journal of molecular biology - 1 Oct 2026

Hashimoto Hideharu, Mawn Ian H, Escobar-Arrillaga William, Nguyen Linh, Madigan Laura A, Antuono Gina, Rossy Tatiana, Sojati Jorna, Mienko Anna, Debler Erik W, Palenchar Jennifer B

Abstract excerpt

Bacterial d-3-hydroxybutyrate dehydrogenases (HBDHs) catalyze the conversion between d-3-hydroxybutyrate and acetoacetate with NAD as the cofactor but not with NAD 2'-phosphate (NADP). However, HBDHs of the early-branched eukaryotic genus Trypanosoma utilize both NAD and NADP (T. brucei) or exclusively NADP (T. cruzi). Here we reveal that NADP specificity of T. cruzi HBDH arises from stabilization of the flexible...

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Kinetics
Models, Molecular
Mutation
NAD
NADP

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Substrate Specificity

Trypanosoma brucei brucei

Trypanosoma cruzi

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Identifiers

PMID: 42456964
DOI: 10.1016/j.jmb.2026.169946
PMCID: PMC13455077

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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