1983
DOI: 10.1073/pnas.80.9.2462
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Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli.

Abstract: The deoxyribonucleotide sequence of pyrB, the cistron encoding the catalytic subunit of aspartate transcarbamoylase (carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2), has been determined. The pyrB gene encodes a polypeptide of 311 amino acid residues initiated by an NH2-terminal methionine that is not present in the catalytically active polypeptide. The DNA sequence analysis revealed the presence of an eightamino-acid sequence beginning at Met-219 that was not detected in previous analyses of a… Show more

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Cited by 66 publications
(45 citation statements)
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“…Codon usage in the archaeal pyrB and pyrI genes is significantly different from that observed in the homologous E. coli genes (30,66). In particular, codons ATA (Ile), AAG (Lys), GAG (Glu), and AGG (Arg) are frequently used in the archaeal genes, while they are rarely used or even absent (AGG) in the E. coli pyrBI operon (a quantitative comparison is available on re- quest).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Codon usage in the archaeal pyrB and pyrI genes is significantly different from that observed in the homologous E. coli genes (30,66). In particular, codons ATA (Ile), AAG (Lys), GAG (Glu), and AGG (Arg) are frequently used in the archaeal genes, while they are rarely used or even absent (AGG) in the E. coli pyrBI operon (a quantitative comparison is available on re- quest).…”
Section: Resultsmentioning
confidence: 99%
“…This dodecameric enzyme (78) is composed of two types of polypeptide chains: the catalytic chains (c) encoded by the pyrB gene (30) and regulatory chains (r) encoded by the pyrI gene (66). The quaternary structure of this enzyme results from the association of two catalytic c3 subunits (trimers of catalytic chains of 310 amino acids; molecular weight, 34,301) held together through their interactions with three regulatory r2 subunits (dimers of regulatory chains of 152 amino acids; molecular weight, 17,109) (8).…”
mentioning
confidence: 99%
“…To the best of our knowledge this is the first instance in which more than one ATCase gene has been isolated from any organism; we refer to the two pea ATCase cDNAs as pyrBl and pyrB2, following the bacterial nomenclature, where the pyrB gene encodes the catalytic subunit of ATCase (Hoover et al, 1983). Restriction maps for the pATC57 and pATC22 cDNAs are shown in Figure 1.…”
Section: Results and Dlscusslon Lsolation And Characterization Of Atcmentioning
confidence: 99%
“…In contrast, cornparison of the amino acid sequence of the pea pyrBl ATCase with that of the catalytic polypeptide of E. coli ATCase (Fig. 2;Hoover et al, 1983) indicates that they are only 3816 identical. However, the sequences that constitute the substrate-binding domains are highly conserved among a11 of the ATCases.…”
Section: Conservation Of Structure In Plant and Bacterial Atcasesmentioning
confidence: 99%
“…The sole exception was a single amino acid deletion in an a-helix at position 183. The residues involved 13,000 33,500 in substrate binding and catalysis in the E. coli enzyme (7-9) 13,943 34,185 were found to be conserved in the CAD sequence ( (28,29); kinetic data (34); other properties (3,6). (9); CAD residues are from sequence homology (Fig.…”
Section: P|v N R G Veji D D S L V E S E K S R I|f|klq|m K|n G|v F|i Rmentioning
confidence: 99%