인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
cis-Aconitate decarboxylase (ACOD1, CAD, IRG1) catalyses the synthesis of itaconic acid in activated myeloid cells such as macrophages. Several histidine residues in the active site bind the substrate and enable the decarboxylation reaction. The in vitro activity of ACOD1 enzymes is commonly determined by incubation with substrate, followed by HPLC measurement of itaconic acid production. Phosphate buffers have often been used for this assay. However, the influence of buffer type on enzyme activity has not been investigated. Here, the effect of buffer and pH on enzyme kinetics of human and mouse ACOD1 and Aspergillus terreus CAD was investigated. It was found that high concentrations of phosphate inhibit the three enzymes. An alternative buffer was selected and the assay was adapted to the 96-well microtitre plate format for increased throughput. Enzyme kinetics were determined in the pH range of 5.5-8.25. A strong increase of K<sub>M</sub> values was observed between the physiologically relevant pH values 7.5 and 8.25. The data indicate that more than one histidine residue needs to be protonated in the active site for binding the substrate.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
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