Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-hydroperoxides from linoleic acid by a pH-dependent mechanism

Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism

Volumn 1001, Issue 3, 1989, Pages 274-281

  Gardner, Harold W ^a  

^a NATIONAL CENTER FOR AGRICULTURAL UTILIZATION RESEARCH   (United States)

Author keywords

(G. max); Linoleic acid hydroperoxide; Lipoxygenase mechanism; pH effect

Indexed keywords

HYDROPEROXIDE; LINOLEIC ACID; LIPOXYGENASE;

HIGHER PLANT; NONHUMAN; PENTADIENE DERIVATIVE; PRIORITY JOURNAL; SOYBEAN;

BINDING SITES; HYDROGEN-ION CONCENTRATION; LINOLEIC ACID; LINOLEIC ACIDS; LIPOXYGENASE; MODELS, CHEMICAL;

EID: 0024562115     PISSN: 00052760     EISSN: None     Source Type: Journal    
DOI: 10.1016/0005-2760(89)90111-2     Document Type: Article

References (50)

1. Crystalline Lipoxidase.
2. Primary structure of soybean lipoxygenase-1.
3. The influence of oxygen on the fluorescence of lipoxygenase
4. Thermal isomerisation of methyl linoleate hydroperoxides. Evidence of molecular oxygen as a leaving group in a radical rearrangement
5. Analysis of a specific oxygenation reaction of soybean lipoxygenase-1 with fatty acids esterified in phospholipids
6. The positional specificity of wheat lipoxygenase; the carboxylic group as signal for the recognition of the site of the hydrogen removal
7. The octadeca-9,12-dienyl sulphate anion; a new, water-soluble substrate for lipoxygenase