Identification and characterisation of a gene encoding aminoacylase activity from Lactococcus lactis MG1363

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TY  - JOUR
  - Curley, P,van Sinderen, D
  - 2000
  - February
  - Fems Microbiology Letters
  - Identification and characterisation of a gene encoding aminoacylase activity from Lactococcus lactis MG1363
  - Validated
  - ()
  - aminoacylase IS982 element Lactococcus lactis BACILLUS-STEAROTHERMOPHILUS THERMOSTABLE AMINOACYLASE NUCLEOTIDE-SEQUENCE MOLECULAR-CLONING ESCHERICHIA-COLI EXPRESSION AMIDOHYDROLASE PURIFICATION PROTEIN ELEMENT
  - 183
  - 177
  - 182
  - Analysis of the sequence of a randomly cloned chromosomal DNA fragment (3.2 kb) from Lactococcus lactis revealed the presence of part of an open reading frame, designated tn,amd1, which specifies a protein displaying significant similarity to aminoacylases from various bacteria. The presence of an immobilised copy of an IS982 element immediately upstream of the coding region of amd1 has probably resulted in the displacement of amd1's native promoter. This genetic organisation was shown to be retained in seven other dairy strains, one of which was only slightly different. The amd1 gene was overexpressed in L. lactis NZ9800 under the control of the inducible nisA promoter and the deacetylating capacity of its gene product was measured on a number of substrates. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
DA  - 2000/02
ER  - 
@article{V43339040,
   = {Curley,  P and van Sinderen,  D },
   = {2000},
   = {February},
   = {Fems Microbiology Letters},
   = {Identification and characterisation of a gene encoding aminoacylase activity from Lactococcus lactis MG1363},
   = {Validated},
   = {()},
   = {aminoacylase IS982 element Lactococcus lactis BACILLUS-STEAROTHERMOPHILUS THERMOSTABLE AMINOACYLASE NUCLEOTIDE-SEQUENCE MOLECULAR-CLONING ESCHERICHIA-COLI EXPRESSION AMIDOHYDROLASE PURIFICATION PROTEIN ELEMENT},
   = {183},
  pages = {177--182},
   = {{Analysis of the sequence of a randomly cloned chromosomal DNA fragment (3.2 kb) from Lactococcus lactis revealed the presence of part of an open reading frame, designated tn,amd1, which specifies a protein displaying significant similarity to aminoacylases from various bacteria. The presence of an immobilised copy of an IS982 element immediately upstream of the coding region of amd1 has probably resulted in the displacement of amd1's native promoter. This genetic organisation was shown to be retained in seven other dairy strains, one of which was only slightly different. The amd1 gene was overexpressed in L. lactis NZ9800 under the control of the inducible nisA promoter and the deacetylating capacity of its gene product was measured on a number of substrates. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.}},
  source = {IRIS}
}
AUTHORSCurley, P,van Sinderen, D
YEAR2000
MONTHFebruary
JOURNAL_CODEFems Microbiology Letters
TITLEIdentification and characterisation of a gene encoding aminoacylase activity from Lactococcus lactis MG1363
STATUSValidated
TIMES_CITED()
SEARCH_KEYWORDaminoacylase IS982 element Lactococcus lactis BACILLUS-STEAROTHERMOPHILUS THERMOSTABLE AMINOACYLASE NUCLEOTIDE-SEQUENCE MOLECULAR-CLONING ESCHERICHIA-COLI EXPRESSION AMIDOHYDROLASE PURIFICATION PROTEIN ELEMENT
VOLUME183
ISSUE
START_PAGE177
END_PAGE182
ABSTRACTAnalysis of the sequence of a randomly cloned chromosomal DNA fragment (3.2 kb) from Lactococcus lactis revealed the presence of part of an open reading frame, designated tn,amd1, which specifies a protein displaying significant similarity to aminoacylases from various bacteria. The presence of an immobilised copy of an IS982 element immediately upstream of the coding region of amd1 has probably resulted in the displacement of amd1's native promoter. This genetic organisation was shown to be retained in seven other dairy strains, one of which was only slightly different. The amd1 gene was overexpressed in L. lactis NZ9800 under the control of the inducible nisA promoter and the deacetylating capacity of its gene product was measured on a number of substrates. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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