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At least 19 recordsLinked to original sources
PubMed1976

Studies on niacin biosynthesis from 3-hydroxyanthranilic acid in streptozotocin diabetic rats in vivo and in vitro.

Biosynthesis of niacin from 3-hydroxyanthranilic acid (3-OHAA) in normal and streptozotocin diabetic rats was studied in vivo and in vitro. Streptozotocin (SZ) diabetic rats were found to excrete lesser quantities of 3-OHAA, quinolinic acid, niacin and N1-methylnicotinamide (nmn) in their urines following 3-OHAA administration than corresponding normal rats. In vitro studies indicated that SZ diabetic livers form less quinolinic acid from 3-OHAA than normal livers. It appears that this may be due to elevated picolinic carboxylase activity in the livers of SZ diabetic rats.

3-Hydroxyanthranilic Acid↗
PubMed1976

Beef kidney 3-hydroxyanthranilic acid oxygenase. Purification, characterization, and analysis of the assay.

Beef kidney 3-hydroxyanthranilic acid oxygenase has been purified to homogeneity. It is a single subunit protein of Mr = 34,000 +/- 2,000 with a frictional coefficient (f/f0) of about 1.1. The enzyme readily aggregates to form, apparently inactive, higher molecular weight oligomers. The very rapid loss of enzyme activity during the assay was analyzed extensively. It was found to be due to inactivation of the enzyme by the substrate, 3-hydroxyanthranilate, and unrelated to enzyme turnover or oxidation of bound iron. The loss of activity was shown to be a first order decay process, and methods are given for obtaining accurate initial reaction rates under all conditions. Evidence was presented that the enzyme assumes a catalytically inactive conformation at pH 3.4, which only relatively slowly rearranges to an active form at pH 6.5; the rearrangement can be blocked by the presence of substrate. We have found that Fe2+, which is required for enzymatic activity, can equilibrate freely, albeit slowly, with the enzyme during the course of the enzyme reaction even in the presence of saturating 3-hydroxanthranilate. Under assay conditons, the Fe2+ has an apparent dissociation constant of 0.04 mM. The kinetic properties of the enzyme were found to be dramatically different in beta,beta-dimethylglutarate buffer and collidine buffer; both the rate of loss of activity during the assay and the substrate Km and Vmax were affected.

Animals↗
PubMed1979

[3-hydroxyanthranilic acid content in the urine of bladder cancer patients].

The work has shown the possibility to determine immunologically 3-OAA-antigen in the urine of bladder cancer patients, which is absent in the urine of healthy individuals. By the identity reaction the authors proved the supposed structure of the detected antigen, i. e. the presence of 3-oxianthranilic acid in it. The data obtained may lie in the basis of the immunodiagnostic test to bladder cancer.

3-Hydroxyanthranilic Acid↗
PubMed1977

[Content of 3-hydroxyanthranilic acid antigens and antibodies in mice in early stages of hepatocarcinogenesis].

By means of a qualitative and quantitative method of precipitation it was found possible to record 3-OAA-antigens in mice receiving ortho-aminoazotoluene. the authors obtained some additional data indicating a similar kinetics of binding for exogenous and endogenous carcinogen. The elaborated method of quantitation of 3-OAA-antigens in the urine may be used for studying the kinetics of this index in cancer patients.

3-Hydroxyanthranilic Acid↗
PubMed1978

Metabolic abnormalities of tryptophan and nicotinic acid in patients with rheumatoid arthritis.

The mean plasma total tryptophan concentration of 13 long-standing rheumatoid arthritis patients was found to be lower than that of seven nonrheumatoid control subjects, but the plasma nicotinic acid concentration was unchanged. In the rheumatoid patients the urinary excretion of the tryptophan metabolites, kynurenine, xanthurenic acid and 3-hydroxyanthranilic acid, was increased several fold, but the excretion of N-methylnicotinamide was normal. These findings are discussed in relationship to the dietary intakes of tryptophan, nicotinic acid and pyridoxine, the effect of antirheumatoid drugs on plasma tryptophan and liver tryptophan pyrrolase, and requirement of rheumatoid patients for pyridoxine.

3-Hydroxyanthranilic Acid↗
PubMed1978

The metabolism of [carboxyl-14C]anthranilic acid. I. The incorporation of radioactivity into NAD+ and NADP+.

A new pathway of NAD+ synthesis from anthranilic acid was found in the livers of rats. Starting from [carboxyl-14C]anthranilic acid, radioactive NAD+ and NADP+ were produced as judged by Dowex-1 X 8-formate column chromatography followed by radiochromatography. Several intermediate compounds, such as quinolinic acid, nicotinic acid mononucleotide, and nicotinic acid adenine dinucleotide were also identified with the aid of various chromatographic techniques. In the experiments with liver microsomal hydroxylation systems, anthranilic acid was converted into not only 5-hydroxyanthranilic acid but also 3-hydroxyanthranilic acid.

Animals↗
PubMed1975

[Studies on tryptophan metabolism in untreated phenylketonuric patients].

The products of the oxidative degradation of tryptophan via the kynurenine pathway were quantitatively determined in the urine of ten untreated patients with phenylketonuria, aged 4--35 years. All the patients were sevrely mentally retarded. The results of the analysis suggest a division of the patients into two groups, A and B. The patients of group A showed a basal urinary excretion of kynurenine, kynurenic acid, 3-hydroxykynurenine and xanthurenic acid which lies in the lower part of the normal range. The increase in excretion of tryptophan metabolites under tryptophan loading was, however, significantly less than in controls. On the average, only 0.63 % of the load was excreted in the form of these assayed metabolites; in contrast, the control value is 1,13 %. In group B, the rate of excretion was higher than normal under basal and loading conditions. The post-tryptophan excretion was four times greater than that of controls (4.64 %). 3-hydroxyanthranilic acid could only be detected in group B after loading. The metabolite 8-hydroxyquinaldic acid, which is supposed to be an abnormal metabolic product of tryptophan, was excreted in milligram amounts. The analysis of the metabolites of 3-hydroxyanthranilic acid showed that the excretion of N1-methylnicotinamide and N1-methyl-2-pyridone-5-carboxamide was within the normal range. The excretion of nicotinic acid and its amide was sporadic in both the patients and controls. Other theoretically possible metabolites in the pathway could not be found. A number of unidentified metabolites could be detected by thin-layer chromatography in the basal state. The excretion of these metabolites was greatly augmented after tryptophan loading. Other substances which were not detectable in the basal state became evident on loading. A number of these metabolites are characteristic either of group A or B. The structural identification of one of the new products has been hindered by its instability. A stable cleavage product was identified as omicron-aminoacetophenon by mass-spectroscopy. This metabolite its typical for group B. The possible influence of the blood phenylalanine on the metabolism of tryptophan in phenylketonuria is discussed.

Acetophenones↗
PubMed1976

Tryptophan metabolism "via" nicotimic acid in patients with scleroderma.

The tryptophan metabolism "via" kynurenine was studied in five patients with scleroderma after aminoacid loading. Four of these patients had abnormal tryptophan metabolism, characterized by a large urinary excretion of kynurenine and kynurenic acid in two cases, of kynurenine, 3-hydroxykynurenine and kynurenic acid in one case and of 3-hydroxyanthranilic acid in another case and generally a reduced excretion of xanthurenic acid and its 8-methyl ether in comparison with a group of healthy controls. Only two of the four patients had a normal response to tryptophan loading after pyridoxine administration, while no one of these responded to nicotinamide supplementation. But the simultaneous administration of pyridoxine and nicotinamide to three of these patients normalized the excretory picture after tryptophan loading. This suggested the presence of a combined vitamin deficiency in seleroderma. As four out of five patients showed total excretory values of kynurenine, kynurenic acid and acetylkynurenine higher than that of the controls, the sum of these values might be considered as a characteristic index of scleroderma.

Adult↗
PubMed1976

[Tryptophan-load in progressive scleroderma (author's transl)].

This presentation describes effects of oral tryptophan loading (5.0 g DL) on tryptophan metabolism in healthy subjects (n = 10) and persons with progressive scleroderma. N1-methylnicotinamide (N1MN), 3-hydroxyanthranilic acid (3 HAA), kynurine (KN), tryptamin (TA), xantheurenic acid (XA) were determinated. Alterations of tryptophan metabolism were evaluated by 24 h urinary excretions of the following metabolites: 5-hydroxy indolacetic acid (5 HAA) and indole-3-acetic acid (IAA). The pathological pathways were discussed, especially the way and influence of serotonine.

3-Hydroxyanthranilic Acid↗
PubMed2026

A horizontally acquired gene mediates insect cocoon pigmentation in the eri silkmoth, Samia ricini.

Holometabolous insects make cocoons during larval-pupal metamorphosis to protect the pupal phase. The materials used for cocoon construction vary widely. Lepidopteran insects typically secrete silk to form cocoons, which display diverse colors. The eri silkworm, Samia cynthia ricini, is an economically important domesticated species that mostly produces white cocoons, with some varieties producing red cocoons. The enzyme kynureninase (KYNU), acquired from bacteria by horizontal gene transfer, has previously been implicated in insect coloration, while the tryptophan metabolite 3-hydroxyanthranilic acid (3-HAA) has been identified as a red pigment. However, exactly how KYNU is involved in cocoon pigmentation remains unclear. Here, we report that a horizontally transferred bacterial gene encoding KYNU regulates red cocoon formation. Metabolomic analysis revealed a high accumulation of 3-HAA in red cocoons, confirming its role as the primary pigment and associating the coloration with tryptophan metabolism. Quantitative real-time polymerase chain reaction (qPCR) analysis indicated that SrKYNU is highly expressed in the silk glands and significantly downregulated in the red cocoon strain compared to the white cocoon strain. Genomic sequencing identified a 141 bp deletion in the upstream regulatory region of KYNU in the red cocoon strain compared to the white cocoon strain. Dual-luciferase assays confirmed that this deletion significantly reduced promoter activity. CRISPR/Cas9 knockout of SrKYNU in the white-cocoon strain resulted in mutants producing red cocoons with elevated 3-HAA content. These findings reveal that the horizontally transferred gene SrKYNU exhibits tissue-specific expression and regulates cocoon coloration in S. ricini, illustrating that horizontal gene transfer can play an important role in regulating an insect physiological process.

Animals↗
PubMedDate not supplied

Inhibition by kynurenine metabolites of proinsulin synthesis in isolated pancreatic islets.

The effect of kynurenine metabolites on insulin biosynthesis was investigated in isolated pancreatic islets of the rat. Both quinaldic acid and 8-hydroxyquinaldic acid were found to produce significant inhibition of the proinsulin synthesis. However, the conversion process of proinsulin to insulin in the islet was not affected by these kynurenine metabolites. Furthermore, the inhibitory effect of these end-metabolites of dynurenine was characterized by preferential inhibition of proinsulin synthesis as distinct from non-insulin protein synthesis in the islet. In contrast to the significant inhibitory effect of quinaldic acid and 8-hydroxyquinaldic acid on proinsulin synthesis, xanthurenic acid and kynurenic acid were far less effective, and L-tryptophan, L-kynurenine, 3-hydroxyanthranilic acid and quinolinic acid showed little ability to inhibit proinsulin synthesis in islets.

Animals↗
PubMed1977

Kinetic studies on 3-hydroxykynureninase from rat liver.

3-Hydroxykynureninase was purified from rat liver. The Michaelis constants for L-kynurenine and L-3-hydroxykynurenine were determined to be 2.33 X 10(-4)M and 6.85 X 10(-5)M, respectively, at pH 8.41 and 37 degrees. With L-kynurenine as substrate, the enzyme was competitively inhibited by L-alanine, 3-hydroxyanthranilic acid, and several other compounds which contained structural features of either amino acid or aryl portions of the substrate. The effect of pH on the initial velocity, maximal velocity, and Michaelis constant, using L-kynurenine as substrate, was studied. Maximal velocity was strongly pH-dependent, with a maximum at pH 8.4. The Michaelis constant decreased from 11.4 X 10(-4)M at pH 7.1 to 1.30 X 10(-4)M at pH 9.0. Logarithmic plots of these data showed pKa's for functional groups ionizing in the enzyme-substrate complex and free enzyme active center of 7.6 and 8.5, respectively. Possible groups responsible for these ionizations were discussed.

Alanine↗
PubMed2026

Metabolic pathways linked to sarcopenia in the Bushehr Elderly Health Program: kynurenine, nicotinamide, B-vitamins, and sulfur amino acids.

BACKGROUND: Sarcopenia, characterized by the loss of muscle mass and function, is a common condition in the elderly, associated with increased morbidity and mortality. Metabolic pathways, including the kynurenine, nicotinamide, B-vitamins, and sulfur amino acid pathways, may play a significant role in the development and progression of sarcopenia. This study investigates the relationship between metabolic pathways and sarcopenia, aiming to identify potential therapeutic targets. METHOD: Four hundred participants over 60 years were randomly selected from the second stage of the Bushehr Elderly Health Program (BEH). Frozen plasma samples were used to measure metabolomics. We used factor analysis and logistic regression analysis to determine the kynurenine-tryptophan metabolites associated with sarcopenia and its components. RESULT: Study participants included 89 sarcopenic subjects aged 72.92 ± 7.32 years and 307 non-sarcopenic subjects aged 68.12 ± 5.56 years. In full model adjustment, factor 3, which included methionine, tryptophan, 3-hydroxyanthranilic acid, picolinic acid, and xanthurenic acid, was associated with 38.3% lower risk of sarcopenia (OR = 0.617 [95%CI = 0.436–0.875]); Factor 6, which included methylmalonic acid and total homocysteine, was associated with a 33.7% increased risk of sarcopenia (OR = 1.337 [95%CI = 1.031–1.735]); and factor 7, consisting of nicotinamide, were related to a 25.2% lower risk of developing sarcopenia (OR = 0.748 [95%CI = 0.571–0.979]). Additionally, factor 1, which included quinolinic acid, kynurenine, 3-hydroxykynurenine, neopterin, kynurenic acid, anthranilic acid, cystathionine, and total cysteine, was linked to a 49.2% higher risk of low muscle strength, while factors 3 and 7 were associated with approximately a 24% decrease in risk of low muscle strength. Factors 5, consisting of serine and glycine, and factor 7 were related to 43% and 27.7% lower risk of low skeletal muscle index, respectively. While factor 6 was related to a 32.8% higher risk of low skeletal muscle index. Factor 1 was also related to a 32.9% higher risk of low walking speed, while factor 3 was related to a 28.5% lower risk of low walking speed. CONCLUSION: Specific metabolites from the kynurenine, nicotinamide, B-vitamin, and sulfur amino acid pathways are significantly associated with sarcopenia and its key parameters, such as muscle strength, skeletal muscle index, and walking speed. These findings suggest that metabolic profiling could offer valuable insights for early detection and targeted interventions for sarcopenia in elderly populations.

Humans↗
PubMed1979

Phenoxazinone biosynthesis: accumulation of a precursor, 4-methyl-3-hydroxyanthranilic acid, by mutants of Streptomyces parvulus.

Mutants of Streptomyces parvulus that are blocked in the synthesis of the phenoxazinone-containing antibiotic, actinomycin, were isolated by the 'agar piece' method (after ultraviolet irradiation or treatment with 8-methoxypsoralen plus near-ultraviolet light). Radiolabelling experiments in conjunction with paper, thin-layer and column chromatography revealed that 4-methyl-3-hydroxyanthranilic acid (MHA) is a major metabolite accumulated by these mutants. Studies in vitro and in vivo provided evidence that MHA is a precursor of the phenoxazinone chromophore, actinocin. Normally MHA does not accumulate during growth or antibiotic synthesis by the parental strains. Protoplasts derived from the mutant strain AM5 synthesized MHA in significant amounts. A scheme is proposed for the biosynthesis of actinomycin D that accounts for the accumulation of MHA by the mutants.

3-Hydroxyanthranilic Acid↗
PubMed1976

[Induction of tyrosine aminotransferase by blastomogenic metabolites of tryptophan and tyrosine].

A comparitive study was made of the effect produced by endogenous blastomogenic agents (3-oxyanthranylic and paraoxphenyl-lactic acids) and their nonblastomogenic anaogues (anthranylic and phenyl-lactic acids) on the activity of tyrosine-aminotranspherase in the rat liver. Blastomogenic metabolites proved to be capable of inducing sharply the enzyme activity. This phenomenon and data on the role played by the increase in the activity of tyrosine-aminotranspherase and tryptophane-oxygenase in tyrosine and tryptophane catabolism on the way of a possible formation of blastomogenic metabolites permitted to put forward a suggestion on the "chain reaction" of accumulation of the endogenous blastomogenic agents in the organism.

3-Hydroxyanthranilic Acid↗
PubMed1977

Cinnabarinate synthase from baboon (Papio ursinus) liver. Identity with catalase.

The enzyme chinnabarinate synthase was purified from the nuclei of baboon liver. Two purified fractions were obtained that exhibited a typical haem protein absorption spectrum; a probable identity with catalase was demonstrated. It was confirmed that catalase in the presence of Mn2+ produces cinnabarinate from 3-hydroxyanthranilate. Doubt is expressed on the existence of a distinct cinnabarinate synthase enzyme.

3-Hydroxyanthranilic Acid↗