2002
DOI: 10.1093/emboj/cdf298
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Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry

Abstract: The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the¯exible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the … Show more

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Cited by 31 publications
(60 citation statements)
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“…A comparison of multiple ASs from a variety of organisms shows that this residue is highly conserved. The crystal structure of the dimeric anthranilate PRT of Sulfolobus solfataricus has been published (30). While Pro362 is not conserved in S. solfataricus, this amino acid is located next to a conserved residue in the proposed anthranilate binding site, R364.…”
Section: Resultsmentioning
confidence: 99%
“…A comparison of multiple ASs from a variety of organisms shows that this residue is highly conserved. The crystal structure of the dimeric anthranilate PRT of Sulfolobus solfataricus has been published (30). While Pro362 is not conserved in S. solfataricus, this amino acid is located next to a conserved residue in the proposed anthranilate binding site, R364.…”
Section: Resultsmentioning
confidence: 99%
“…The overall three-dimensional structure of anthranilate phosphoribosyltransferase is similar among all of the species so far analyzed, i.e., the enterobacterium Pectobacterium carotovorum (286), S. solfataricus (284), M. tuberculosis (285), Xanthomonas campestris (PDB code 4hkm), T. thermophilus (PDB code 1v8g), and a cyanobacterial species (Nostoc sp.) (PDB code 1vqu).…”
Section: Reactions At the Anomeric Carbon Of Prppmentioning
confidence: 94%
“…The anthranilate phosphoribosyltransferase isolated from E. coli is bifunctional: it also contains glutamine chorismate amidotransferase activity. Consequently, the E. coli trpD gene product is considerably larger, a total of 531 amino acid residues, than monofunctional anthranilate phosphoribosyltransferases, such as those from S. solfataricus or M. tuberculosis, which have 345 or 370 amino acid residues, respectively (284,285). Other tryptophan biosynthetic enzymes from various species have been shown to harbor two activities.…”
Section: Reactions At the Anomeric Carbon Of Prppmentioning
confidence: 99%
“…The pathway of Trp biosynthesis is the first amino acid pathway for which the atomic structure of every catalytic domain has been determined (58), a circumstance of significance because evolutionary analysis can be greatly enhanced through insight gained at the structural level of protein folding. Consultation of the reference by Yanofsky et al (97) is highly recommended for a definitive presentation of the detailed literature up to about Nomenclature is at the level of catalytic domain in order of reaction steps in the pathway.…”
Section: Biochemical Pathway Of Tryptophan Biosynthesismentioning
confidence: 99%