Enzymatic characterization of a nonmotile, nonsolventogenicClostridium acetobutylicum ATCC 824 mutant

Autor:	Daniel J. Petersen, George N. Bennett
Rok vydání:	1991
Předmět:	chemistry.chemical_classification Clostridium acetobutylicum biology Mutant Dehydrogenase General Medicine biology.organism_classification Applied Microbiology and Biotechnology Microbiology Cofactor Enzyme assay Enzyme Biochemistry chemistry Acetoacetate decarboxylase biology.protein Flagellin
Zdroj:	Current Microbiology. 23:253-258
ISSN:	1432-0991 0343-8651
DOI:	10.1007/bf02092026
Popis:	Decreased motility has been correlated with lower solvent yields in fermentations withClostridium acetobutylicum. A spontaneous mutant ofC. acetobutylicum was found to be nonmotile as evidenced by bright-field microscopy and motility-agar plates. The loss of motility was accompanied by the production of an altered flagellin. The mutant flagellin was much smaller than the wild-type (32 vs 43 kDa), although the NH2-terminal amino acid sequences of both flagellins were identical. This mutant was simultaneously incapable of producing the solvents acetone and butanol. In vitro enzyme activity analyses demonstrated the absence of three enzymes directly involved in solvent production: acetoacetate decarboxylase (EC 4.1.1.4), acetoacetyl-coenzyme A:acetate/butyrate coenzyme A-transferase (EC 2.8.3.9), and NADP-dependent butyraldehyde dehydrogenase (EC 1.2.1.10).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::5feb5d2b6cfcdaad4a6d3bdd3b6ce51b https://doi.org/10.1007/bf02092026 Zobrazit plný text záznamu Full text from SpringerLink