Regiochemical and Stereochemical Evidence for Enzyme-initiated Catalysis in Dual Positional Specific Maize Lipoxygenase-1.
From: Department of Molecular Biotechnology, Biotechnology Research Institute, College of Agriculture and Life Sciences, Chonnam National University, Kwangju 500-757, Republic of Korea.
Organic letters
- Publish Date: Aug 2007
- ISSN: 1523-7060
- Volume: 9
- Issue: 16
- Pages: 3113-6
- Medium: Print
- Language: English
- Citation (JAMA): Jang Sungkuk, Huon Thavrak, Kim Keumhwa, et al. Regiochemical and Stereochemical Evidence for Enzyme-initiated Catalysis in Dual Positional Specific Maize Lipoxygenase-1.. Org. Lett. Aug 2007;9:3113-6
Abstract
Dual positional specific maize lipoxygenase-1 catalyzed the formation of racemic mixtures of four possible regioisomers and was strongly inhibited by the radical scavenger, 4-hydroxy-2,2,6,6-tetramethyl-1-piperidinoxy radical. Molecular modeling studies indicated that the oxygen-binding cavity is segregated from the substrate-binding cavity. The data suggest that a bis-allylic radical reaction intermediate is generated enzymatically, released from the enzyme active site, and subsequently oxygenated outside of the enzyme active site by a nonenzymatic mechanism.
Mesh Headings (Keywords): Binding Sites, Catalysis, Cyclic N-Oxides, Free Radical Scavengers, Lipoxygenase, Molecular Structure, Spin Labels, Stereoisomerism, Zea mays
Check for Full Text / PubMed Unique Identifier (PMID): 17629290
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.