Cited by 208Bacterial Genetics and BiotechnologyBiochemical and Molecular ResearchAmino Acid Enzymes and Metabolism

Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci

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Smith, D K, Kassam, T, Singh, B, Elliott, J F·1992·Journal of Bacteriology

Abstract

Degenerate oligonucleotides based on the published Escherichia coli glutamate decarboxylase (GAD) protein sequence were used in a polymerase chain reaction to generate a DNA probe for the E. coli GAD structural gene. Southern blots showed that there were two cross-hybridizing GAD genes, and both of these were cloned and sequenced. The two GAD structural genes, designated gadA and gadB, were found to be 98% similar at the nucleotide level. Each gene encoded a 466-residue polypeptide, named, respectively, GAD alpha and GAD beta, and these differed by only five amino acids. Both GAD alpha and GAD beta contain amino acid residues which are highly conserved among pyridoxal-dependent decarboxylases, but otherwise the protein sequences were not homologous to any other known proteins. By restriction mapping and hybridization to the Kohara miniset library, the two GAD genes were located on the E. coli chromosome. gadA maps at 4046 kb and gadB at 1588 kb. Neither of these positions is in agreement with the current map position for gadS as determined by genetic means. Analysis of Southern blots indicated that two GAD genes were present in all E. coli strains examined, including representatives from the ECOR collection. However, no significant cross-hybridizing gene was found in Salmonella species. Information about the DNA sequences and map positions of gadA and gadB should facilitate a genetic approach to elucidate the role of GAD in E. coli metabolism.

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Crossref · 10.1128/jb.174.18.5820-5826.1992

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  • Both host and bacteria have the capacity to convert the amino acid glutamate to GABA.

    “Both host and bacteria have the capacity to convert the amino acid glutamate to GABA (Smith et al., 1992;Strandwitz et al., 2019)”

    From The Microbiota-Gut-Brain Axis (2019) · cites this paper as Smith et al., 1992

    The paper’s Abstract describes two glutamate decarboxylase genes in E. coli, supporting the bacterial capacity attributed to it. Our copy mentions human glutamate decarboxylases only in a cited reference; it does not establish the host’s capacity to convert glutamate to GABA. (LLM, conf=0.74)

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Cited by

Sorted by citations

Authors
Smith, D. K., Kassam, T., Singh, B., & Elliott, J. F.
Affiliations
University of Alberta (CA)
Venue
Journal of Bacteriology
Published
1992-09
Volume
174
Issue
18
Pages
5820-5826
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
OpenAlex
W1498871304
Cited by
208
References
0
Citations by year
2025: 6 · 2024: 2 · 2023: 9 · 2022: 9 · 2021: 5 · 2020: 6 · 2019: 6 · 2018: 7 · 2017: 7 · 2016: 6 · 2015: 4 · 2014: 9 · 2013: 12 · 2012: 7
FWCI
2.19
Type
journal article
Language
en
Open access
Locations
  • Journal of Bacteriology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
Association pour la Recherche sur le Diabète
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords
Escherichia coli, glutamic acid decarboxylase, GADA, gadB, gene homology, gene mapping, chromosomal localization, GAD, glutamate metabolism, Salmonella
MeSH terms
Amino Acid Sequence, Base Sequence, Escherichia coli, Genes, Bacterial, Multigene Family, Glutamate Decarboxylase, Isoenzymes, Molecular Sequence Data, Nucleic Acid Hybridization, Sequence Homology, Nucleic Acid, Restriction Mapping

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