Abstract
γ-Aminobutyric acid (GABA) is a non-proteinous amino acid with some functions for human health. In this study, aminoaldehyde dehydrogenase (EC 1.2.1.19, AMADH) which has been proven to be an essential enzyme responsible for the GABA bioformation via polyamine degradation pathway was purified from 2-day germinated soybeans and characterized. The partially purified enzyme showed a single major band with a relative molecular mass of approximately 53.72 kDa-subunit using sodium dodecyl sulfate gel electrophoresis. AMADH exhibited the optimal activity at pH 8.0 and at 45 °C, respectively. The activity of purified AMADH was significantly inhibited by some heavy metal ions and sulfhydryl reagents. The cDNA of AMADH was sequenced by RT-PCR, which indicated 1,677 bp long and contained a 1,515 bp open reading frame that encoded 504 amino-acid peptides (GenBank accession number: KC478661).
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.