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Sentences for "anthranilate"
psittaci is incomplete in that genes encoding the two subunits of anthranilate synthase ( trpAa and trpAb ) are absent.
psittaci lacks anthranilate synthase.
It is of interest that the conversion of kynurenine to anthranilate and the conversion of 3-hydroxykynurenine to 3-hydroxyathranilate are similar hydrolytic reactions.
In addition to extra-operonic, free-standing copies of trpAa and trpAb , a second fused gene ( trpAa • trpAb_2 ) encoding the two domains of anthranilate synthase is present in Anabaena .
These include the overall gene organization of the trp operon, for which many microbial patterns are known, the extremely rare gene order of trpEa trpEb instead of the typical order trpEb trpEa, the fusion of genes encoding the alpha ( trpAa ) and beta ( trpAb ) subunits of anthranilate synthase, a fusion that exists in only a limited number of other taxa, and the presence of operonic genes exhibiting distinctive homology subtypes ( aroA Iß and tyrA (p) ).
Within the low-GC block, trpR is separated by four ORFs from genes encoding the two subunits of anthranilate synthase ( trpAa and trpAb ).
Genes encoding the two anthranilate synthase subunits ( trpAa and trpAb ) and aryl-CoA ligase ( acl ) surely belong to an operon, as translational coupling is evident from the overlap of start and stop codons (Figure 4).
Because acl is tightly organized with trpAa and trpAb , it seems feasible that anthranilate might be the substrate of acl .
If anthranilate is indeed the substrate of Acl in Xylella , it would be a futile cycle if anthranilate were formed biosynthetically, only to be subsequently catabolized.
Therefore, it seems more likely that the activation of anthranilate could be a step in the formation of a siderophore or antibiotic compound that is assembled by a nonribosomal peptide synthetase mechanism (see Quadri et al .
This comprises an anthranilate synthase that is not strictly required for primary tryptophan biosynthesis and that is uniquely expressed during stationary-phase physiology [ 40].
Why the generation of anthranilate under these conditions would be of value is unknown, but phylogenetic trees clearly show phnA/phnB to be xenologs originating from the enteric lineage via LGT (G.
The Xylella genes are associated with other genes that presumably dictate a fate for anthranilate other than as a primary precursor of tryptophan.
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