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8X8F

Crystal structure of lipoxygenase from Enhygromyxa salina

Summary for 8X8F
Entry DOI10.2210/pdb8x8f/pdb
DescriptorArachidonate 15-lipoxygenase, CADMIUM ION (3 entities in total)
Functional Keywords9-lipoxygenase, oxidoreductase
Biological sourceEnhygromyxa salina
Total number of polymer chains12
Total formula weight852446.57
Authors
Kim, J.W.,Seo, P.W.,Kim, J.S. (deposition date: 2023-11-27, release date: 2024-11-27, Last modification date: 2025-12-17)
Primary citationKim, J.W.,Yoon, J.H.,Lee, J.,Cha, H.J.,Seo, P.W.,Lee, T.E.,Bornscheuer, U.T.,Oh, D.K.,Park, J.B.,Kim, J.S.
Discovery and Molecular Characterization of a Novel 9 S -Lipoxygenase from Enhygromyxa salina for Fatty Acid Biotransformations.
J.Agric.Food Chem., 72:26263-26273, 2024
Cited by
PubMed Abstract: Iron-dependent lipoxygenases (LOXs) are involved in the synthesis of oxylipins from polyunsaturated fatty acids. However, they are usually difficult to overexpress in functional form in microbial cell factories. Moreover, 9-LOXs, generating 9-hydroperoxy fatty acids from C18 polyunsaturated fatty acids, have rarely been found from microbial sources. Here, we discovered a novel 9-LOX in the marine myxobacterium (Es-9-LOX). The recombinant enzyme produced in exhibited remarkable activity in the dioxygenation of linoleic acid (LA, ), α-linolenic acid, γ-linolenic acid, and arachidonic acid specifically at the C9 position to yield the product with ()-configuration at catalytic efficiency of 3.94, 1.42, 1.38, and 0.69 μM·s, respectively. The elucidated X-ray crystal structure of Es-9-LOX reveals a long and narrow hydrophobic pocket that allows the substrate to be near the metal ion and the oxygen tunnel. The enzyme was successfully used in a chemoenzymatic reaction to generate a hydroxy fatty acid from LA. Our study thus contributes to the valorization of renewable polyunsaturated fatty acids into a variety of fatty acid derivatives, including hydroxy fatty acids.
PubMed: 39536131
DOI: 10.1021/acs.jafc.4c01258
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.796 Å)
Structure validation

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