Purification and characterization of glyoxalase I from Pseudomonas putida |
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| Authors: | H Rhee K Murata A Kimura |
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| Affiliation: | 1. CSIR- Indian Institute of Integrative Medicine, Sanatnagar, Srinagar, Kashmir, India;2. Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India;3. Department of Biotechnology, Babasaheb Bhimrao Ambedkar University, Vidya Vihar, Raebareli Road, Lucknow 226025, Uttar Pradesh, India;4. Medicinal Chemistry Division, CSIR-Indian Institute of Integrative Medicine, Jammu, India;5. High Content Imaging Facility, CSIR-Indian Institute of Integrative Medicine, India;6. Cancer Pharmacology Division, CSIR-Indian Institute of Integrative Medicine, Jammu, India |
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| Abstract: | Glyoxalase I was purified to apparent homogeneity from Pseudomonas putida. The enzyme was a monomer with a molecular weight of 20,000. The enzyme was most active at pH 8.0. The Km values for methylglyoxal and 4,5-dioxovale-rate are 3.5 mM and 1.2 mM, respectively. Contrary to the case of eukaryotic enzymes, chelating agents showed little inhibitory effects on the enzyme activity. Among the metal ions tested, Zn++ specifically and completely inhibited the activity of the enzyme at a millimolar level. The properties of bacterial glyoxalase I were quite different from mammalian and yeast enzymes. |
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