Purification and properties of an ld-dipeptidase FROM Bacillus sphaericus |
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| Institution: | 1. College of Life and Environmental Science, Wenzhou University, Wenzhou 325035, China;2. Key Laboratory of Vector Biology and Pathogen Control of Zhejiang Province, Huzhou University, Huzhou Cent Hosp, Huzhou 313000, China;1. Key Laboratory of Animal Models and Human Disease Mechanisms and Engineering Laboratory of Peptides of Chinese Academy of Sciences, Key Laboratory of Bioactive Peptides of Yunnan Province, KIZ-CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, National Resource Center for Non-Human Primates, National Research Facility for Phenotypic & Genetic Analysis of Model Animals (Primate Facility), and Sino-African Joint Research Center, New Cornerstone Science Institute, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China;2. College of Life Science, Zhengzhou University, Zhengzhou, Henan 450001, China;3. First Affiliated Hospital of Kunming Medical University, Kunming 650032, China;4. Kunming College of Life Science, University of Chinese Academy of Sciences, Beijing 100049, China;1. Anesthesia and Intensive Care, San Martino Policlinico Hospital, IRCCS for Oncology and Neuroscience, Genoa, Italy;2. Department of Anesthesiology and Intensive Care Medical University of Lublin, 20-954 Lublin, Poland;3. Department of Surgical Sciences and Integrated Diagnostic (DISC), University of Genoa, Genoa, Italy;4. Laboratory of Pulmonary Investigation, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, RJ, Brazil;1. State Key Laboratory of Genetic Engineering, Greater Bay Area Institute of Precision Medicine (Guangzhou), School of Life Sciences and Human Phenome Institute, Fudan University, Shanghai 200438, China;2. Wenzhou Center for Disease Control and Prevention, Wenzhou, Zhejiang 325002, China;3. Wuhan Center for Disease Control and Prevention, Wuhan, Hubei 430022, China;4. Longquan Center for Disease Control and Prevention, Longquan, Zhejiang 323799, China;5. Sydney Institute for Infectious Diseases, School of Medical Sciences, The University of Sydney, Sydney, NSW 2006, Australia;6. Laboratory of Data Discovery for Health Limited, Hong Kong SAR, China |
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| Abstract: | - 1.1. An ld-dipeptidase (EC 3.4.13.-) that hydrolyzes the unrelated dipeptides l-Ala-d-Glu (sp. act. 0.85 μmol·min?1·mg?1) and l-Lys-d-Ala (sp. act. 11 μmol · min?1·mg?1) has been purified 250-fold from the sporulation medium of Bacillus sphaericus with a 4% recovery of lytic activity.
- 2.2. Throughout the purification steps, followed with both substrates, the enzyme peaks of activities were congruent and the ratios of activities were constant. Both activities were activated 50-fold by cobalt. Polyacrylamide gel electrophoresis of the final preparation showed the two enzyme activities to be coincident. The data are consistent with those activities being due to a single enzyme.
- 3.3. Sodium dodecylsulfate polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band (Mr 38,000).
- 4.4. This dipeptidase hydrolyzes some other ld-dipeptides with a free amino and carboxyl group. Although dipeptides having a di-amino acid as the amino terminus are the best of the substrates tested, the hydrolysis occurs also when neutral amino acids are N-terminal. The activity is higher with neutral C-terminal residues such as Gly or d-Ala than with a di-acid residue such as d-Glu.
- 5.5. This enzyme may have a function in peptidoglycan metabolism.
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