Lee, KS Chi, YM Yu, YG 2024-01-21T11:09:35Z 2024-01-21T11:09:35Z 2021-09-05 2002-02 1017-7825 https://pubs.kist.re.kr/handle/201004/139828 The effect of pressure on the catalytic properties of glutamate racemase from Aquifiex pyrophilus, an extremophilic bacterium, was investigated. The activation volume for the overall reaction (DeltaV(not equal)) and catalysis (DeltaV(cat)(not equal)) was -96.97 ml/ mol and 4.97 mt/mol, respectively, while the reaction volume for the substrate binding (DeltaV(km)(-1)) was - 101.94 ml/mol. The large negative DeltaV(not equal) for the overall reaction indicated that the pressurization of glutamate racemase resulted in enhanced catalytic efficiencies. In addition, this value was also due to the large negative DeltaV(km)(-1) for the substrate binding. The negative value of DeltaV(km)(-1) implied that the conformational changes in the enzyme molecule occurred during the substrate binding process, thereby increasing the degree of hydration. The small value of DeltaV(cat)(not equal) suggested that the pressure did not affect the glutamate racemase catalysis after the substrate binding. English KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY ENZYMATIC CATALYSIS ACTIVATION ENZYMES MICROORGANISMS VOLUMES Effect of pressure on catalytic properties of glutamate racemase from Aquifex pyrophilus, an extremophilic bacteria Article 1 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.12, no.1, pp.149 - 152 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 12 1 149 152 scie scopus kci 000174286600024 Biotechnology & Applied Microbiology Microbiology Biotechnology & Applied Microbiology Microbiology Article ENZYMATIC CATALYSIS ACTIVATION ENZYMES MICROORGANISMS VOLUMES activation volume Aquifex pyrophilus extremophiles glutamate racemase high pressure