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Article

Probing the Electrostatic and Steric Requirements for Substrate Binding in Human Platelet-Type 12-Lipoxygenase.

Biochemistry - 12 Feb 2019

Aleem Ansari Mukhtar, Tsai Wan-Chen, Tena Jennyfer, Alvarez Gabriella, Deschamps Joshua, Kalyanaraman Chakrapani, Jacobson Matthew P, Holman Theodore

Abstract excerpt

Human platelet ALOX12 (hALOX12 or h12-LOX) has been implicated in a variety of human diseases. The present study investigates the active site of hALOX12 to more thoroughly understand how it positions the substrate and achieves nearly perfect regio- and stereospecificities (i.e., 100 ± 5% of the 12(S)-hydroperoxide product), utilizing site-directed mutagenesis. Specifically, we have determined that Arg402 is not...

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Source

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Identifiers

PMID: 30565457
DOI: 10.1021/acs.biochem.8b01167
PMCID: PMC7270147

Genes

ALOX12
LOX

Provenance

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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Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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