Department of Biochemistry, University of Saskatchewan, S7N OWO, Saskatoon, Saskatchewan, Canada.
Plant Cell Rep. 1985 Aug;4(4):206-9. doi: 10.1007/BF00269290.
Studies to determine the role of histidine in catalysis by L-argininosuccinate synthetase (EC 6. 3. 4. 5) were carried out with the enzyme isolated from soybean cell suspension cultures. These experiments utilized analogues of the substrates citrulline and aspartate to investigate substrate binding, and to determine which portion of the molecule were required for binding at the active site of the enzyme. Photooxidation studies using rose bengal were carried out to define the importance of histidine residues for catalysis. These studies suggest that an active site histidine residue has an important role to play in the formation of argininosuccinate by this enzyme.
研究确定组氨酸在 L-精氨琥珀酸合成酶(EC 6.3.4.5)催化中的作用,使用从大豆细胞悬浮培养物中分离的酶进行了这些研究。这些实验利用瓜氨酸和天冬氨酸的类似物来研究底物结合,并确定分子的哪一部分是在酶的活性部位结合所必需的。使用玫瑰红进行光氧化研究,以确定组氨酸残基对催化的重要性。这些研究表明,一个活性部位的组氨酸残基在该酶形成精氨琥珀酸中起着重要作用。