Em plantas a AASADH é codificada pelo gene Aldh7a1 e o gene é bastante conservado entre plantas e animais.
Ensaios de western-blot em condições denaturantes mostraram que a AASADH de milho possui aproximadamente 54 kDa, mas na forma ativa se apresenta na forma de tetrâmero.
Como previsto no modelo da via da sacaropina, o AASA foi transformado em AAA mediante a redução do cofator NAD a NADH. Além disso, a enzima foi seletiva quanto ao cofator, não apresentando atividade na presença de NADP.
A enzima de endosperma de milho pode efetivamente transformar AASA em AAA; Estudos cinéticos com a AASADH de milho mostraram que a enzima é capaz de metabolizar diversos outros aldeídos além do AASA;
LKR/SDH e AASADH são co-expressas no endosperma em desenvolvimento, mas não em embriões e tecidos vegetativos, onde só AASADH é detectada;
Em coleóptilos, AASADH e LKR/SDH são induzidas por estresse salino, osmótico e oxidativo ao nível da transcrição, mas apenas AASADH produz proteína traduzida – AASADH pode estar envolvida em processos de detoxificação de aldeídos produzidos em condição de estresse;
Níveis de sacaropina e ácido aminoadípico aumentan no endosperma tratado com lisina, mas diminuem com NaCl. Pipecolato e prolina diminuem com lisina, sugerindo inibição da P5CR. Ao nível da transcrição não há mudanças significativas, possivelmente porque o ambiente na semente já está estressado e a via está totalmente ativa;
O nível de pipecolato é muito inferior que prolina e esta pode ser usada como osmoprotetor em endosperma de milho. O pipecolato pode estar envolvido em resposta a estresse biótico (resposta contra patógenos e herbívoros).
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