tailieunhanh - Báo cáo khoa học: Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum

The fermentation ofb-alanine by Clostridium propionicumproceeds via activation to the CoA-thiol ester, followed by deamination to acryloyl-CoA, which is also an intermediate in the fermentation ofl-alanine. By shifting the organism from the carbon and energy source a-alanine to b-alanine, the enzyme b-alanyl-CoA:ammonia lyase is induced 300-fold ( 30% of the soluble protein). The low basal lyase activity is encoded by theacl1gene, whereas the almost identicalacl2gene (six amino acid substi-tutions) is responsible for the high activity after growth on b-alanine | ềFEBS Journal Two beta-alanyl-CoA ammonia lyases in Clostridium propionicum Gloria Herrmann1 Thorsten Selmer1 Holly J. Jessen2 Ravi R. Gokarn2 Olga Selifonova2 Steve J. Gort2 and Wolfgang Buckel1 1 Laboratorium fur Mikrobiologie Fachbereich Biologie Philipps-Universitat Marburg Germany 2 Biotechnology Development Center CargillIncorporated Minneapolis MN USA Keywords acryloyl-CoA beta-alanyl-CoA CoA-transferase L-alanine and beta-alanine fermentation pentamer Correspondence W. Buckel Laboratorium fur Mikrobiologie Fachbereich Biologie Philipps-Universitat 35032 Marburg Germany Fax 49 64212828979 Tel 49 6421 28 21527 E-mail buckel@ Received 15 October 2004 revised 24 November 2004 accepted 7 December 2004 doi The fermentation of b-alanine by Clostridium propionicum proceeds via activation to the CoA-thiol ester followed by deamination to acryloyl-CoA which is also an intermediate in the fermentation of L-alanine. By shifting the organism from the carbon and energy source a-alanine to b-alanine the enzyme b-alanyl-CoA ammonia lyase is induced 300-fold w 30 of the soluble protein . The low basal lyase activity is encoded by the acll gene whereas the almost identical acl2 gene six amino acid substitutions is responsible for the high activity after growth on b-alanine. The deduced b-alanyl-CoA ammonia lyase proteins are related to putative b-aminobutyryl-CoA ammonia lyases involved in lysine fermentation and found in the genomes of several anaerobic bacteria. b-Alanyl-CoA ammo-nia lyase 2 was purified to homogeneity and characterized as a heteropentamer composed of 16 kDa subunits. The apparent Km value for acryloyl-CoA was measured as 23 4 pM independent of the concentration of the second substrate ammonia kcat Km was calculated as 107 M-1-s-1. The apparent Km for ammonia was much higher 70 5 mM at 150 IM acry-loyl-CoA with a much lower kcat Km of 4 X 103 M-1-s-1. In the reverse reaction a Km of 210 30 pM was .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• genetics
• Structural biochemistry
• Structural Biology
• biology
• biological research
• applied biology
• modern biology
• biological engineering research
• metazoan systems
• Biochemistry cell and molecular biology test
• Molecular Biology Test
• Biochemistry Test
• Genetics test
• Cupramolecular complexes
• Campbell biology
• Biology systems
• Lecture Biology
• Biological sciences
• Molecular basis of inheritance
• Structural model of DNA
• scientific research
• molecular Biology
• structural information
• breast cancer
• BMC Bioinformatics
• Structural systems biology
• Oxidative stress
• Structural proteome
• Physicochemical properties
• Oxidative damage
• Metabolic model
• BMC Molecular and Cell Biology
• HIV 2 protease
• Drug resistance mutations
• Structural asymmetry
• Structural alphabet
• Structural variation
• Structural mutation
• 450 kb duplications
• Kidney cells
• Genome Biology
• Complex structural rearrangements
• Sequence analysis
• Copy number variant
• Tạp chí khoa học
• Structural basis of light energy
• Electron transfer in biology
• Models for energy and electron transfer
• Electron transfer in biological materials
• The blue multi copper
• Biological organization
• Systems biology
• Structural bioinformatics
• Integrative systems biology
• Bioinformatics methods
• Mass spectrometry
• medical reports
• thesis report
• health education
• medical report