Chen Hongwen, Nie Jinfeng, Chen Guo, Fang Baishan
Key Laboratory of Industrial Biotechnology, Fujian Province, Huaqiao University, Xiamen, China.
Sheng Wu Gong Cheng Xue Bao. 2010 Feb;26(2):177-82.
The kinetic mechanisms of two key enzymes in the biotransformation of glycerol to 1,3-propanediol (1,3-PD) by Klebsiella pneumoniae, glycerol dehydrogenase (GDH) and 1,3-propanediol oxidoreductase (PDOR), was characterized. Kinetics on initial velocity and product inhibition revealed that GDH and PDOR follow an ordered Bi-Bi sequential mechanism. Kinetic models for GDH and PDOR showed that the oxidation reaction catalyzed by GDH was the rate-limiting step in coupled enzymatic reaction when the GDH/PDOR was 1:1, and the NAD+ was the main form of coenzyme in the reaction. Knowledge about the kinetic mechanisms will be helpful to understand how these enzymes is regulated, which will be useful for further enzyme catalysis and metabolic engineering studies.
对肺炎克雷伯氏菌将甘油生物转化为1,3 - 丙二醇(1,3 - PD)过程中的两种关键酶,即甘油脱氢酶(GDH)和1,3 - 丙二醇氧化还原酶(PDOR)的动力学机制进行了表征。对初始速度和产物抑制的动力学研究表明,GDH和PDOR遵循有序的双底物双产物顺序机制。GDH和PDOR的动力学模型表明,当GDH/PDOR为1:1时,GDH催化的氧化反应是偶联酶促反应中的限速步骤,并且NAD⁺是该反应中辅酶的主要形式。关于动力学机制的知识将有助于理解这些酶是如何被调节的,这对于进一步的酶催化和代谢工程研究将是有用的。