<p>Type II LDH/MDH oxidoreductases represent a group of enzymes involved in diverse metabolic processes. In eukaryotes, <i>AqE</i> genes encoding these enzymes have been primarily documented in non-terrestrial plants and animals. Genomic analysis of the Pacific oyster <i>Magallana gigas</i> (Thunberg, 1793) revealed three <i>AqE</i> genes. The close genomic proximity of <i>AqE2</i> and <i>AqE3</i> suggests a relatively recent duplication event, supported by their conserved exon-intron organization, predicted protein properties, and phylogenetic clustering. Tree topology further indicates that <i>AqE1</i> and <i>AqE2</i>/<i>AqE3</i> homologs – residing on distinct chromosomes – diverged prior to the split of deuterostomes and protostomes. Despite their shared origin, <i>M. gigas AqE</i> homologs exhibit functional divergence post-duplication: <i>AqE1</i> retains broad tissue/stage specificity (supposed housekeeping role), while <i>AqE2</i> and <i>AqE3</i> show enhanced developmental stage- and tissue-specific expression (supposed special functions). Given the absence of lactate dehydrogenase genes (LDH) in M. gigas and other bivalves, a hypothesis is proposed that AqE gene products may participate in lactate-pyruvate interconversion. These findings establish a foundation for future studies on type II LDH/MDH oxidoreductase evolution, including functional characterization of <i>AqE</i> protein products and analysis of their regulatory elements.</p>

错误:搜索内容不能为空,请输入英文关键词
错误:关键词超出字数限制,请精简
高级检索

Type II LDH/MDH Oxidoreductases in Pacific Oyster Magallana gigas (Thunberg, 1793): Gene Organization and Expression Patterns During Development and Across Tissues

  • Mikhail V. Puzakov,
  • Ludmila V. Puzakova,
  • Polina M. Puzakova,
  • Igor O. Babenko

摘要

Type II LDH/MDH oxidoreductases represent a group of enzymes involved in diverse metabolic processes. In eukaryotes, AqE genes encoding these enzymes have been primarily documented in non-terrestrial plants and animals. Genomic analysis of the Pacific oyster Magallana gigas (Thunberg, 1793) revealed three AqE genes. The close genomic proximity of AqE2 and AqE3 suggests a relatively recent duplication event, supported by their conserved exon-intron organization, predicted protein properties, and phylogenetic clustering. Tree topology further indicates that AqE1 and AqE2/AqE3 homologs – residing on distinct chromosomes – diverged prior to the split of deuterostomes and protostomes. Despite their shared origin, M. gigas AqE homologs exhibit functional divergence post-duplication: AqE1 retains broad tissue/stage specificity (supposed housekeeping role), while AqE2 and AqE3 show enhanced developmental stage- and tissue-specific expression (supposed special functions). Given the absence of lactate dehydrogenase genes (LDH) in M. gigas and other bivalves, a hypothesis is proposed that AqE gene products may participate in lactate-pyruvate interconversion. These findings establish a foundation for future studies on type II LDH/MDH oxidoreductase evolution, including functional characterization of AqE protein products and analysis of their regulatory elements.