Nucleotide sequence and characterization of the gene for secreted alkaline phosphatase from Lysobacter enzymogenes
العنوان: | Nucleotide sequence and characterization of the gene for secreted alkaline phosphatase from Lysobacter enzymogenes |
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المؤلفون: | Kenneth L. Roy, S Au, R. G. Von Tigerstrom |
المصدر: | Journal of Bacteriology. 173:4551-4557 |
بيانات النشر: | American Society for Microbiology, 1991. |
سنة النشر: | 1991 |
مصطلحات موضوعية: | Signal peptide, Molecular Sequence Data, Phosphatase, Biology, Microbiology, Bacterial Proteins, Sequence Homology, Nucleic Acid, Gram-Negative Bacteria, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Codon, Molecular Biology, Peptide sequence, Gel electrophoresis, Base Composition, Base Sequence, Structural gene, Nucleic acid sequence, Alkaline Phosphatase, Molecular biology, Molecular Weight, Open reading frame, Biochemistry, Genes, Bacterial, Alkaline phosphatase, Cattle, Research Article |
الوصف: | Lysobacter enzymogenes produces an alkaline phosphatase which is secreted into the medium. The gene for the enzyme (phoA) was isolated from a recombinant lambda library. It was identified within a 4.4-kb EcoRI-BamH1 fragment, and its sequence was determined by the chain termination method. The structural gene consists of an open reading frame which encodes a 539-amino-acid protein with a 29-residue signal sequence, followed by a 119-residue propeptide, the 281-residue mature phosphatase, and a 110-residue carboxy-terminal domain. The roles of the propeptide and the carboxy-terminal peptide remain to be determined. A molecular weight of 30,000 was determined for the mature enzyme from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The amino acid sequence was compared with sequences available in the current protein data base, and a region of the sequence was found to show considerable homology with sequences in mammalian type 5 iron-containing purple acid phosphatases. |
تدمد: | 1098-5530 0021-9193 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3094cc57df469fabb871af6860611c7b https://doi.org/10.1128/jb.173.15.4551-4557.1991 |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....3094cc57df469fabb871af6860611c7b |
قاعدة البيانات: | OpenAIRE |
تدمد: | 10985530 00219193 |
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