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PubMed1991

Molecular characterization and expression analysis of the anthranilate synthase gene of Pseudomonas syringae subsp. savastanoi.

The trpE gene, which encodes the large component of the enzyme anthranilate synthase, was isolated from a Pseudomonas syringae subsp. savastanoi (P. savastanoi) cosmid library. Cosmids that complemented an Escherichia coli trpE mutation contained a gene whose product is 86% homologous at the deduced amino acid level to TrpE of Pseudomonas aeruginosa and Pseudomonas putida. Amino acid sequence comparison with other TrpE sequences revealed the existence of conserved regions between the procaryotic and eucaryotic polypeptide sequences analyzed, regions that might be of functional importance. We also report on studies on the expression pattern of this gene. We analyzed the promoter activity of a trpE::lacZ transcriptional fusion, the relative amount of trpE steady-state mRNA, and the activity of anthranilate synthase from cells grown in minimal medium with or without exogenously added tryptophan and in complete medium. We concluded that under the conditions tested, expression of the trpE gene of P. savastanoi is independent of the concentration of tryptophan in the culture medium. Implications of such an expression pattern on the virulence of this bacterium are discussed.

Amino Acid Sequence↗
PubMed1993

Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries. Identification and sequencing of the trpEG (D) operon.

Random sequencing of cDNA and genomic libraries has been used to study the genome of the hyperthermophile Thermotoga maritima. To date, 175 unique clones have been analyzed by comparing short sequence tags with known proteins in the PIR and GenBank databases. We find that a significant proportion of sequences can be matched to previously identified protein from non-Thermotoga sources. A high match rate was obtained from an oligo(dT)-primed cDNA library, where one-third of all unique sequences analyzed (21/65) shared high amino acid sequence similarity with proteins in the PIR and GenBank databases. Also, approximately one-third of the unique sequences from a second cDNA library (28/89), constructed with random oligo primers, could be matched to sequences in PIR and GenBank. Identification of genes from the oligo(dT)-primed cDNA library indicates that some Thermotoga mRNAs are polyadenylated. Genes have also been identified from a 1 to 2 kb genomic DNA library. Here, (3/21) of genomic sequences analyzed could be matched to protein in PIR and GenBank. One of the genomic clones had high sequence similarity to the tryptophan synthesis gene anthranilate synthase component I (trpE). Using this sequence tag, the Thermotoga trp operon was isolated and sequenced. The Thermotoga maritima trp operon is arranged with trpE forming an overlapping transcript with a second protein consisting of a fusion of anthranilate synthase component II (trpG) and anthranilate phosphoribosyltransferse (trpD). With regard to the fusion, the operon organization is similar to Escherichia coli and Salmonella typhimurium, but lacks the classic attenuation system of enteric bacteria. Amino acid sequence comparison with 19 trpE, 18 trpG and 14 trpD genes from other organisms suggest that the Thermotoga trp genes resemble corresponding genes from other thermophiles more closely than expected.

Amino Acid Sequence↗
PubMed1981

Effect of tryptophan metabolites and metal ions on the purified kynureninase from rat liver.

Kynureninase purified from rat liver was inhibited by 3-hydroxyanthranilate, or anthranilate, and slightly by 5-hydroxyanthranilate. However, tryptophan metabolites other than anthranilate and its derivatives, and also alpha-keto acids and alanine did not affect the activity of this enzyme. Kynureninase was also inhibited and inactivated by metal ions, especially Hg2+ and Zn2+. On the other hand Mg2+, Ca2+ and monovalent cations had no effect on the activity of the enzyme. The reductants, such as dithiothreitol, reduced glutathione and mercaptoethanol, prevented this inactivation. p-Chloromercurybenzoate (CMB) and N-ethylmaleimide inhibited the enzyme action. Kynureninase which had been completely inactivated by Hg2+ or CMB could be reactivated with excess dithiothreitol, indicating that enzyme inactivation can be attributed to the blocking of sulfhydryl groups. Five sulfhydryl groups per subunit of the enzyme molecule were detected using CMB and mercury orange.

Animals↗
PubMed1994

Unexpected sequence similarity between nucleosidases and phosphoribosyltransferases of different specificity.

Amino acid sequences of enzymes that catalyze hydrolysis or phosphorolysis of the N-glycosidic bond in nucleosides and nucleotides (nucleosidases and phosphoribosyltransferases) were explored using computer methods for database similarity search and multiple alignment. Two new families, each including bacterial and eukaryotic enzymes, were identified. Family I consists of Escherichia coli AMP hydrolase (Amn), uridine phosphorylase (Udp), purine phosphorylase (DeoD), uncharacterized proteins from E. coli and Bacteroides uniformis, and, unexpectedly, a group of plant stress-inducible proteins. It is hypothesized that these plant proteins have evolved from nucleosidases and may possess nucleosidase activity. The proteins in this new family contain 3 conserved motifs, one of which was found also in eukaryotic purine nucleosidases, where it corresponds to the nucleoside-binding site. Family II is comprised of bacterial and eukaryotic thymidine phosphorylases and anthranilate phosphoribosyltransferases, the relationship between which has not been suspected previously. Based on the known tertiary structure of E. coli thymidine phosphorylase, structural interpretation was given to the sequence conservation in this family. The highest conservation is observed in the N-terminal alpha-helical domain, whose exact function is not known. Parts of the conserved active site of thymidine phosphorylases and anthranilate phosphoribosyltransferases were delineated. A motif in the putative phosphate-binding site is conserved in family II and in other phosphoribosyltransferases. Our analysis suggests that certain enzymes of very similar specificity, e.g., uridine and thymidine phosphorylases, could have evolved independently. In contrast, enzymes catalyzing such different reactions as AMP hydrolysis and uridine phosphorolysis or thymidine phosphorolysis and phosphoribosyl anthranilate synthesis are likely to have evolved from common ancestors.

Amino Acid Sequence↗
PubMed1975

Studies on 3-hydroxykynureninase from rat liver.

Kynureninase (L-kynurenine hydrolase E.C. 3.7.1.3.) was purified about 200 times from rat liver. The purified enzyme catalyzes the L-3-hydroxykynurenine leads to 3-hydroxyanthranilate reaction more favorably than the L-kynurenine leads to anthranilate reaction, with Km values of 1.67 x 10(-6) M for L-3-hydroxykynurenine and of 1.67 x 10(-4) M for L-kynurenine. Besides, this enzyme did not produce 5-hydroxyanthranilate from D,L-5-hydroxykynurenine. Therefore we think it is mainly a 3-hydroxykynureninase regulating the tryptophan degradation towards the formation of nicotinic acid necessary to NAD synthesis, rather than towards the accumulation of anthranilate.

Animals↗
PubMed1976

Bilirubin conjugates in bile of man, rat and dog. Semi-quantitative analysis of bile composition by thin-layer chromatography.

1. Conjugated bile pigments, separated in two fractions by semi-quantitative t.l.c. performed on silicic acid with phenol/water as the developing solvent, were treated with diazotized ethyl anthranilate. Resulting dipyrrylazo derivatives were analysed by quantitative t.l.c. 2. The tentative structure elucidation of tetrapyrrolic bilirubin conjugates and semi-quantitative evaluation of rat bile, post-obstructive human bile and dog bile composition is presented. 3. Homogeneous and mixed hexuronic acid diesters of bilirubin containing glucuronic acid constitute 51% of the total conjugates in normal rat bile, 45% of those in human post-obstructive bile and 38% of those in obstructed rat biles. 4. Monoconjugated bilirubin amounts to 33% of total conjugated bile pigments in normal rat bile, and 17 and 14% in post-obstructive hepatic human bile and gall-bladder bile of dog respectively. After loading with unconjugated bilirubin a greater amount of monoconjugates (56%) occur in the rat bile, whereas bilirubin diglucuronide excretion is decreased (34%). 5. In gall-bladder bile of normal dog, 40% of glucose-containing diconjugates, 32% of homogeneous and/or mixed hexuronic acid (mainly glucuronic acid) diesters of bilirubin and 14% of xylose-containing diconjugates are estimated. 6. Increased amounts of bilirubin conjugates, including some with unidentified uronic acid groups, were observed in cholestatic rat biles and quantities of conjugates with glucuronic acid were decreased.

Animals↗
PubMed1978

Amino acid sequence of a peptide containing an essential cysteine residue of Escherichia coli GMP synthetase.

The amino acid sequence of a 51-residue tryptic peptide of citraconylated [1-14C]carboxamidomethyl-labeled Escherichia coli GMP synthetase was determined by sequenator analyses of the intact peptide and fragments obtained by cleavage of the peptide with cyanogen bromide, trypsin, and Staphylcoccus aureus strain V8 protease. The cysteine residue of this peptide fragment is essential for glutamine-dependent GMP synthesis activity and is implicated in formation of a hypothetical covalent glutamyl-enzyme intermediate. There is essentially cysteine-containing regions of two other glutamine amidotransferases, Pseudomonas putida anthranilate synthetase Component II and chicken liver formylglycinamide ribonucleotide amidotransferase. There is, however, a cluster of amino acids with "antipathy" for helix formation and a "nonessential" cysteine of anthranilate synthetase Component II.

Amino Acid Sequence↗
PubMed1996

Factors affecting the metabolism of cinnamyl anthranilate in the rat and mouse.

The biological actions of cinnamyl anthranilate are dependent on both dose size and animal species. The present study aimed to examine metabolism as a possible source of explanation for these differences. [3-14C]Cinnamyl anthranilate was synthesized, injected ip into male Fischer 344 (F344) rats and CD-1 mice and urine and faeces collected for 3 days. The pattern of elimination of 14C was the same in both species, with the bulk of the administered material recovered in urine over the first 24 hr. Urinary metabolic profiles were compared by radioHPLC, which showed that the major radioactive excretion product in the rat was hippuric acid accompanied by smaller amounts of benzoic acid. In contrast, mouse urine contained relatively less hippuric acid, more benzoic acid and small amounts (approx. 3% of dose) of unchanged cinnamyl anthranilate. The effect of dose size on urinary metabolites produced by mice was examined using both 3-14C-labelled and unlabelled cinnamyl anthranilate, detected by fluorescence HPLC. Over a dose range of 5 to 250 mg/kg body weight administered ip it was found that at 5 mg/kg body weight no intact ester was excreted in urine whereas at 20 mg/kg body weight or above, the proportion present as the intact ester remained constant. Dietary administration to male and female B6C3F1 mice for 21 days over a dose range of 0 to 30,000 ppm revealed the same qualitative picture with no intact cinnamyl anthranilate detected in urine at or below 1000 ppm (equivalent to 100 mg/kg body weight). A study in human volunteers using a single oral dose of 250 mg failed to reveal any intact cinnamyl anthranilate in 0-24-hr urine. These data support the hypothesis that the peroxisome proliferating action of cinnamyl anthranilate, which is mediated by the intact ester, is manifest only at high doses in species in which its metabolism by hydrolysis is saturated, as a consequence of which the intact ester 'overflows' into urine.

Adult↗
PubMed1980

[Growth inhibition by phenylalanine and tyrosine--metabolism of phenylalanine in Flavobacterium devorans (author's transl)].

Growth of a chloramphenicol-resistant mutant of Flavobacterium devorans (F. devorans r) was inhibited by L-phenylalanine and L-tyrosine and furthermore by L-tryptophan, 4-amino-benzoate, anthranilate and homogentisate. The inhibitionwas reversed partially by simultaneous addition of aromatic amino acids and 4-amino-benzoate. After cultivating F. devorans r in a glucose-minimal medium containing L-phenylalanine, the metabolites L-tyrosine, 4-hydroxyphenylpyruvate, 4-hydroxyphenylacetate, 4-hydroxybenzaldehyd, 4-hydroxybenzoate, homogentisate and anthranilate were found. Growth inhibition and a hypothetical degrading pathway of phenylalanine are discussed.

Aminobenzoates↗
PubMed1994

Amplification of trpEG: adaptation of Buchnera aphidicola to an endosymbiotic association with aphids.

Survival of aphids is dependent on an association with a prokaryotic endosymbiont (Buchnera aphidicola) found in specialized cells within the aphid body cavity. Recent nutritional and physiological studies have indicated that one of the functions of the endosymbionts is the synthesis of tryptophan [Douglas, A. E. & Prosser, W. A. (1992) J. Insect Physiol. 38, 565-568]. B. aphidicola resembles in many of its properties free-living prokaryotes. An adaptation to an endosymbiosis involving the overproduction of tryptophan would necessitate alterations that modify the effect of regulatory systems that in free-living organisms function to reduce enzyme activity under conditions of excess tryptophan. We have cloned and sequenced the genes for B. aphidicola trpEG encoding anthranilate synthase, the first enzyme of the tryptophan biosynthetic pathway, which in free-living bacteria is feedback-inhibited by tryptophan. Amino acid sequence comparisons indicate that the B. aphidicola enzyme has all of the key residues involved in allosteric feedback inhibition. Evidence is presented indicating that trpEG is present as four tandem repeats on a circular plasmid. Relative to B. aphidicola trpDC(F)BA (the chromosomal genes coding for the remaining enzymes of the tryptophan biosynthetic pathway) trpEG is amplified 14- to 15-fold. These findings suggest that the effect of inhibition by accumulated tryptophan may be overcome by overproduction of anthranilate synthase. Our results demonstrate the acquisition of a new property (gene amplification) as an adaptation to an endosymbiotic association in which B. aphidicola overproduces tryptophan for the aphid host.

Amino Acid Sequence↗
PubMed1977

Mycophenolic acid and its mechanism of action in cancer and psoriasis.

Mycophenolic acid is active against fungi, bacteria, and viruses in vitro and is active against some viruses and tumors in experimental animals. Mycophenolic acid is not effective in the treatment of cancer in man, but it is effective in treating psoriasis. In all of the various diseases MA presumably inhibits the synthesis of GMP resulting in decreased synthesis of RNA and DNA. The direct inhibition of GMP synthesis is the result of MA activity against the IMPDHase and GMP synthetase as determined in experimental tumors. The inhibition of GMP synthesis can be circumvented by the guanine salvage pathway which is controlled by PRTase activity. PRTase may be the sole factor in preventing the inhibition caused by MA in the biosynthesis of GMP (Fig. 3). However, before MA can stop GMP synthesis, MA must enter the cell. The current data show that MA is almost completely detoxified in man and circulates in the plasma as the glucuronide, MAG, Glucuronides are normally inactive forms of active drugs. Due to their bivalent and non-lipophilic nature, glucuronides do not normally cross the cell membranes. Therefore, MAG is extracellular and beta-Gase intracellular, and this prevents hydrolysis of MAG to the active MA in cancer patients.

Animals↗
PubMed2003

Cloning and sequence analysis of the TRP1 gene encoding the phosphoribosyl anthranilate isomerase from Pichia anomala (strain K).

Pichia anomala (strain K) is an efficient biocontrol agent against post-harvest diseases affecting apples. To study the role of strain K genes in biocontrol activity, it is useful to identify selectable markers on which to base a gene disruption strategy. The Pichia anomala TRP1 gene (PaTRP1) was isolated by complementation of the multi-auxotrophic S. cerevisiae strain FY-1679-18b. DNA sequence analysis revealed the presence of a 699 bp ORF encoding a 233 amino acid protein showing the typical conserved structure of proteins of the phosphoribosyl anthranilate isomerase (PRAI) family. Codon analysis revealed a high number of unused codons. Downstream from PaTRP1 was found the 3' extremity of a gene highly similar to the IPP1 gene (coding for the inorganic pyrophosphatase).

Aldose-Ketose Isomerases↗
PubMed2005

A Link between ethylene and auxin uncovered by the characterization of two root-specific ethylene-insensitive mutants in Arabidopsis.

The plant hormone ethylene participates in the regulation of a variety of developmental processes and serves as a key mediator of plant responses to biotic and abiotic stress factors. The diversity of ethylene functions is achieved, at least in part, by combinatorial interactions with other hormonal signals. Here, we show that ethylene-triggered inhibition of root growth, one of the classical effects of ethylene in Arabidopsis thaliana seedlings, is mediated by the action of the WEAK ETHYLENE INSENSITIVE2/ANTHRANILATE SYNTHASE alpha1 (WEI2/ASA1) and WEI7/ANTHRANILATE SYNTHASE beta1 (ASB1) genes that encode alpha- and beta-subunits of a rate-limiting enzyme of Trp biosynthesis, anthranilate synthase. Upregulation of WEI2/ASA1 and WEI7/ASB1 by ethylene results in the accumulation of auxin in the tip of primary root, whereas loss-of-function mutations in these genes prevent the ethylene-mediated auxin increase. Furthermore, wei2 and wei7 suppress the high-auxin phenotypes of superroot1 (sur1) and sur2, two auxin-overproducing mutants, suggesting that the roles of WEI2 and WEI7 in the regulation of auxin biosynthesis are not restricted to the ethylene response. Together, these findings reveal that ASA1 and ASB1 are key elements in the regulation of auxin production and an unexpected node of interaction between ethylene responses and auxin biosynthesis in Arabidopsis. This study provides a mechanistic explanation for the root-specific ethylene insensitivity of wei2 and wei7, illustrating how interactions between hormones can be used to achieve response specificity.

Anthranilate Synthase↗