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Article

Identification of structural determinants of NAD(P)H selectivity and lysine binding in lysine N(6)-monooxygenase.

Archives of biochemistry and biophysics - 15 Sept 2016

Abdelwahab Heba, Robinson Reeder, Rodriguez Pedro, Adly Camelia, El-Sohaimy Sohby, Sobrado Pablo

Abstract excerpt

l-lysine (l-Lys) N(6)-monooxygenase (NbtG), from Nocardia farcinica, is a flavin-dependent enzyme that catalyzes the hydroxylation of l-Lys in the presence of oxygen and NAD(P)H in the biosynthetic pathway of the siderophore nocobactin. NbtG displays only a 3-fold preference for NADPH over NADH, different from well-characterized related enzymes, which are highly selective for NADPH. The structure of NbtG with...

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Identifiers

PMID: 27503802
DOI: 10.1016/j.abb.2016.08.004

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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