TY - JOUR
T1 - Nucleotide sequence and deduced amino add sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein
AU - Grabau, Charlotte
AU - Cronan, John E.
N1 - Funding Information:
ACKNOWLEDGEMENTS We thank J. Mankovlch for helpful advice on DNA sequencing, M. Recny, S. Hamilton, and L. Hager for sharing their amino acid sequence data before publication, Y.-Y. Chang for helpful discussions concerning the protein homology, R. Gesteland for the use of hi3 laboratory facilities for the synthesis of oligonucleotides, and R. S. Wolfe for the use of his computer during part of this work. This work wa3 supported by National Science Foundation Grant PCM 8308778 and a National Institute of Health Traineeship (GM 07283). We acknowledge BIONET National Computer Resource for Molecular Biology, whose funding is provided by the Biomedical Research Technology Program Division of Research Resources NIH Grant I 1U41RRQ1685-02.
PY - 1986/7/11
Y1 - 1986/7/11
N2 - The entire nucleotide sequence of the poxB (pyruvate oxidase) gene of Eseherichia coli K-12 has been determined by the dideoxynucleotide (Sanger) sequencing of fragments of the gene cloned into a phage M13 vector. The gene is 1716 nucleotides In length and has an open reading frame which encodes a protein of Mr 62,018. This open reading frame was shown to encode pyruvate oxidase by alignment of the amino acid sequences deduced for the amino and carboxy termini and several internal segments of the mature protein with sequences obtained by amino acid sequence analysis. The deduced amino acid sequence of the oxidase was not unusually rich in hydrophobic sequences despite the peripheral membrane location and lipid binding properties of the protein. The codon usage of the oxidase gene was typical of a moderately expressed protein. The deduced amino acid sequence shares homology with the large subunits of the acetohydroxy acid synthase isozymes I, II,and III, encoded by the ilvB, ilvG, and ilvI genes of E. coli.
AB - The entire nucleotide sequence of the poxB (pyruvate oxidase) gene of Eseherichia coli K-12 has been determined by the dideoxynucleotide (Sanger) sequencing of fragments of the gene cloned into a phage M13 vector. The gene is 1716 nucleotides In length and has an open reading frame which encodes a protein of Mr 62,018. This open reading frame was shown to encode pyruvate oxidase by alignment of the amino acid sequences deduced for the amino and carboxy termini and several internal segments of the mature protein with sequences obtained by amino acid sequence analysis. The deduced amino acid sequence of the oxidase was not unusually rich in hydrophobic sequences despite the peripheral membrane location and lipid binding properties of the protein. The codon usage of the oxidase gene was typical of a moderately expressed protein. The deduced amino acid sequence shares homology with the large subunits of the acetohydroxy acid synthase isozymes I, II,and III, encoded by the ilvB, ilvG, and ilvI genes of E. coli.
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U2 - 10.1093/nar/14.13.5449
DO - 10.1093/nar/14.13.5449
M3 - Article
C2 - 3016647
AN - SCOPUS:0023046885
SN - 0305-1048
VL - 14
SP - 5449
EP - 5460
JO - Nucleic acids research
JF - Nucleic acids research
IS - 13
ER -