Discovery of Methyl-End Desaturases in Razor Clam Sinonovacula constricta (Lamarck 1818) and Their Spatio-Temporal Expression.

Chen, Xinyi; Fang, Xiang; Yang, Dongzi; Xu, Jilin; Ran, Zhaoshou

Clarifying the biosynthetic pathway of the long-chain polyunsaturated fatty acids (LC-PUFA) of Sinonovacula constricta is essential for utilizing its LC-PUFA resources. Methyl-end (or "ωx") desaturases are the rate-limiting enzymes in LC-PUFA biosynthesis, catalyzing the conversion of oleic acid to linoleic acid (LA) or LA to α-linolenic acid. However, their presence in S. constricta remains uncertain. Herein, we identified two ωx desaturase-like genes within the S. constricta genome, both located on the ninth chromosome possibly due to genome duplication. These genes exhibited nearly identical sequences, differing by only one amino acid, and each encodes a 354-residue peptide with typical ωx desaturase characteristics. Phylogenetic analysis grouped these putative ωx desaturases with similar enzymes from other invertebrates. However, when heterologously expressed in yeast, they exhibited no detectable desaturation activity. This suggests either non-functionality in yeast or extremely subtle desaturation abilities. Additionally, both genes displayed the highest expression in the inhalant siphon rather than in digestive tissues and exhibited relatively high expression throughout the development stages of S. constricta, except in zygotes. These findings suggest potential in vivo functional roles for these ωx desaturases in S. constricta. Collectively, these results significantly enrich our understanding of the repertoire of LC-PUFA biosynthetic enzymes in this important bivalve species.

UNSATURATED fatty acids; DESATURASES; PEPTIDES; OLEIC acid; AMINO acids; LINOLEIC acid

Fishes (MDPI AG), 2024, Vol 9, Issue 9, p359

2410-3888

Academic Journal

10.3390/fishes9090359