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Article

Structural elements contribute to the calcium/calmodulin dependence on enzyme activation in human endothelial nitric-oxide synthase.

The Journal of biological chemistry - 26 Dec 2003

Chen Pei-Feng, Wu Kenneth K

Abstract excerpt

Two regions, located at residues 594-606/614-645 and residues 1165-1178, are present in the reductase domain of human endothelial nitric-oxide synthase (eNOS) but absent in its counterpart, inducible nitric-oxide synthase (iNOS). We previously demonstrated that removing residues 594-606/614-645 resulted in an enzyme (Delta45) containing an intrinsic calmodulin (CaM) purified from an Sf9/baculovirus expression...

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Identifiers

PMID: 14561757
DOI: 10.1074/jbc.M305469200

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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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