Molecular cloning and nucleotide sequence of the gene encoding phosphate-inducible pectin lyase of Bacillus subtilis. 1996

T Sakamoto, and H Kawasaki, and T Sakai
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University, Sakai, Japan. sakamoto@envi.osakafu-u.ac.jp

The gene encoding the pectin lyase (PNL; EC 4.2.2.10) of Bacillus subtilis has been cloned, sequenced, and characterized. A coding sequence for the PNL composed of 345 amino acids including a 24-amino-acid signal peptide was assigned. No sequence resembling a LexA binding site was found upstream of the structural gene. Furthermore, PNL activity of the gene product expressed in Escherichia coli DH5alpha was detected intracellularly, which might suggest that expression of the gene was not controlled by RecA. Regulation of the gene expression seemed to be quite different from that of other bacterial PNL genes previously reported.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010368 Pectins High molecular weight polysaccharides present in the cell walls of all plants. Pectins cement cell walls together. They are used as emulsifiers and stabilizers in the food industry. They have been tried for a variety of therapeutic uses including as antidiarrheals, where they are now generally considered ineffective, and in the treatment of hypercholesterolemia. Calcium Pectinate,Methoxy Pectin,Methoxylpectin,Methoxypectin,Pectin,Pectinic Acid,Zinc Pectinate,Pectin, Methoxy,Pectinate, Calcium,Pectinate, Zinc
D010710 Phosphates Inorganic salts of phosphoric acid. Inorganic Phosphate,Phosphates, Inorganic,Inorganic Phosphates,Orthophosphate,Phosphate,Phosphate, Inorganic
D011133 Polysaccharide-Lyases A group of carbon-oxygen lyases. These enzymes catalyze the breakage of a carbon-oxygen bond in polysaccharides leading to an unsaturated product and the elimination of an alcohol. EC 4.2.2. Polysaccharide Lyase,Polysaccharide-Lyase,Lyase, Polysaccharide,Polysaccharide Lyases
D011938 Rec A Recombinases A family of recombinases initially identified in BACTERIA. They catalyze the ATP-driven exchange of DNA strands in GENETIC RECOMBINATION. The product of the reaction consists of a duplex and a displaced single-stranded loop, which has the shape of the letter D and is therefore called a D-loop structure. Rec A Protein,RecA Protein,Recombinases, Rec A
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D004790 Enzyme Induction An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis. Induction, Enzyme
D005798 Genes, Bacterial The functional hereditary units of BACTERIA. Bacterial Gene,Bacterial Genes,Gene, Bacterial
D006031 Glycosylation The synthetic chemistry reaction or enzymatic reaction of adding carbohydrate or glycosyl groups. GLYCOSYLTRANSFERASES carry out the enzymatic glycosylation reactions. The spontaneous, non-enzymatic attachment of reducing sugars to free amino groups in proteins, lipids, or nucleic acids is called GLYCATION (see MAILLARD REACTION). Protein Glycosylation,Glycosylation, Protein

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