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Volumn 58, Issue 9, 2003, Pages 829-836

Enzyme activities of tryptophan metabolism along the kynurenine pathway in various species of animals

Author keywords

Animal species; Kynurenine pathway enzymes; Tryptophan metabolism

Indexed keywords

3 HYDROXYANTHRANILATE 3,4 DIOXYGENASE; AMINOCARBOXYMUCONATE SEMIALDEHYDE DECARBOXYLASE; APOENZYME; ENZYME; INDOLE 2,3 DIOXYGENASE; INTESTINE ENZYME; KIDNEY ENZYME; KYNURENINASE; KYNURENINE 3 MONOOXYGENASE; KYNURENINE AMINOTRANSFERASE; LIVER ENZYME; SUPEROXIDE DISMUTASE; TRYPTOPHAN 2,3 DIOXYGENASE; UNCLASSIFIED DRUG;

EID: 0141788065     PISSN: 0014827X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-827X(03)00140-X     Document Type: Article
Times cited : (33)

References (59)
  • 1
    • 0001868532 scopus 로고
    • Aspects of disorders of the kynurenine pathway of tryptophan metabolism in man
    • Musajo L., Benassi C.A. Aspects of disorders of the kynurenine pathway of tryptophan metabolism in man. Adv. Clin. Chem. 7:1964;63-135.
    • (1964) Adv. Clin. Chem. , vol.7 , pp. 63-135
    • Musajo, L.1    Benassi, C.A.2
  • 2
    • 0013819226 scopus 로고
    • Testing the functional capacity of the tryptophan-niacin pathway in man by analysis of urinary metabolites
    • Price J.M., Brown R.R., Yess N. Testing the functional capacity of the tryptophan-niacin pathway in man by analysis of urinary metabolites. Adv. Metab. Disord. 2:1965;159-225.
    • (1965) Adv. Metab. Disord. , vol.2 , pp. 159-225
    • Price, J.M.1    Brown, R.R.2    Yess, N.3
  • 3
    • 0016007501 scopus 로고
    • Studies on tryptophan metabolism in man
    • Wolf H. Studies on tryptophan metabolism in man. Scand. J. Clin. Lab. Invest. Suppl. 136:1974;1-186.
    • (1974) Scand. J. Clin. Lab. Invest. Suppl. , vol.136 , pp. 1-186
    • Wolf, H.1
  • 4
    • 0026044893 scopus 로고
    • Tryptophan nutrition and metabolism: An overview
    • R. et al. Schwarcz. New York: Plenum Press
    • Peters J.C. Tryptophan nutrition and metabolism: an overview. Schwarcz R., et al. Kynurenine and Serotonin Pathways. 1991;345-358 Plenum Press, New York.
    • (1991) Kynurenine and Serotonin Pathways , pp. 345-358
    • Peters, J.C.1
  • 5
    • 0001209055 scopus 로고
    • A clinical, physiologic and biochemical study of patients with malignant carcinoid (argentaffinoma)
    • Sjoerdsma A., Weissback H., Udenfriend S. A clinical, physiologic and biochemical study of patients with malignant carcinoid (argentaffinoma). Am. J. Med. 20:1956;520-532.
    • (1956) Am. J. Med. , vol.20 , pp. 520-532
    • Sjoerdsma, A.1    Weissback, H.2    Udenfriend, S.3
  • 6
    • 0013941673 scopus 로고
    • Urinary excretion of indoxyl sulphate (indican) by human subjects ingesting a semisynthetic diet containing variable quantities of L-tryptophan
    • Bryan G.T. Urinary excretion of indoxyl sulphate (indican) by human subjects ingesting a semisynthetic diet containing variable quantities of L-tryptophan. Am. J. Clin. Nutr. 19:1966;113-119.
    • (1966) Am. J. Clin. Nutr. , vol.19 , pp. 113-119
    • Bryan, G.T.1
  • 7
    • 0003068068 scopus 로고
    • Formation of indole-3-acetic acid and tryptamine in animals. A method for estimation of indole-3-acetic acid in tissues
    • Weissbach H., King W., Sjoerdsma A., Udenfriend S. Formation of indole-3-acetic acid and tryptamine in animals. A method for estimation of indole-3-acetic acid in tissues. J. Biol. Chem. 234:1959;81-86.
    • (1959) J. Biol. Chem. , vol.234 , pp. 81-86
    • Weissbach, H.1    King, W.2    Sjoerdsma, A.3    Udenfriend, S.4
  • 9
    • 0016224141 scopus 로고
    • Melanogenesis from tryptophan. Biogenetic experiments with Harding-Passey mouse melanoma
    • De Antoni A., Allegri G., Costa C., Bordin F. Melanogenesis from tryptophan. Biogenetic experiments with Harding-Passey mouse melanoma. Experientia. 30:1974;600-601.
    • (1974) Experientia , vol.30 , pp. 600-601
    • De Antoni, A.1    Allegri, G.2    Costa, C.3    Bordin, F.4
  • 10
    • 0016585867 scopus 로고
    • Studies on melanogenesis of tryptophan in Harding-Passey mouse melanoma
    • Costa C., Allegri G., De Antoni A. Studies on melanogenesis of tryptophan in Harding-Passey mouse melanoma. Acta Vitaminol. Enzymol. 29:1975;223-226.
    • (1975) Acta Vitaminol. Enzymol. , vol.29 , pp. 223-226
    • Costa, C.1    Allegri, G.2    De Antoni, A.3
  • 11
    • 0017211365 scopus 로고
    • Problems and proposals on the study of tryptophan metabolism
    • Chiancone F.M., Allegri G. Problems and proposals on the study of tryptophan metabolism. Acta Vitaminol. Enzymol. 30:1976;130-133.
    • (1976) Acta Vitaminol. Enzymol. , vol.30 , pp. 130-133
    • Chiancone, F.M.1    Allegri, G.2
  • 12
    • 0018235124 scopus 로고
    • A further contribution to the choice of the dose for l-tryptophan load test
    • Allegri G., Costa C., De Antoni A. A further contribution to the choice of the dose for l-tryptophan load test. Acta Vitaminol. Enzymol. 32:1978;163-166.
    • (1978) Acta Vitaminol. Enzymol. , vol.32 , pp. 163-166
    • Allegri, G.1    Costa, C.2    De Antoni, A.3
  • 13
    • 0013824145 scopus 로고
    • Tryptophan-pyrrolase, kynureninase and kynurenine transaminase activities of human renal tumors
    • Allegri G., Benassi C.A., Boccù E., De Nadai A., Perissinotto B. Tryptophan-pyrrolase, kynureninase and kynurenine transaminase activities of human renal tumors. Br. J. Cancer. 19:1965;754-760.
    • (1965) Br. J. Cancer , vol.19 , pp. 754-760
    • Allegri, G.1    Benassi, C.A.2    Boccù, E.3    De Nadai, A.4    Perissinotto, B.5
  • 14
    • 0030332977 scopus 로고    scopus 로고
    • Occurence of indoleamine 2,3-dioxygenase in human cutaneous malignant melanoma
    • Bertazzo A., Costa C.V.L., Lise M., Nitti D., Allegri G. Occurence of indoleamine 2,3-dioxygenase in human cutaneous malignant melanoma. Adv.Exp. Med. Biol. 398:1996;519-522.
    • (1996) Adv.Exp. Med. Biol. , vol.398 , pp. 519-522
    • Bertazzo, A.1    Costa, C.V.L.2    Lise, M.3    Nitti, D.4    Allegri, G.5
  • 15
    • 0022354604 scopus 로고
    • Human indolylamine 2,3-dioxygenase. Its tissue distribution and characterization of the placental enzyme
    • Yamakazi F., Kuroiwa T., Takikawa O., Kido R. Human indolylamine 2,3-dioxygenase. Its tissue distribution and characterization of the placental enzyme. Biochem. J. 230:1985;635-638.
    • (1985) Biochem. J. , vol.230 , pp. 635-638
    • Yamakazi, F.1    Kuroiwa, T.2    Takikawa, O.3    Kido, R.4
  • 16
    • 0026050510 scopus 로고
    • Kynureninase and kynurenine 3-hydroxylase in mammalian tissues
    • R. et al. Schwarcz. New York: Plenum Press
    • Okuno E., Kido R. Kynureninase and kynurenine 3-hydroxylase in mammalian tissues. Schwarcz R., et al. Kynurenine and Serotonin Pathways. 1991;167-176 Plenum Press, New York.
    • (1991) Kynurenine and Serotonin Pathways , pp. 167-176
    • Okuno, E.1    Kido, R.2
  • 17
  • 18
    • 0014217450 scopus 로고
    • Tryptophan pyrrolase of rabbit intestine d- and l-tryptophan cleaving enzyme or enzymes
    • Yamamoto S., Hayaishi O. Tryptophan pyrrolase of rabbit intestine d- and l-tryptophan cleaving enzyme or enzymes. J. Biol. Chem. 242:1967;5260-5266.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5260-5266
    • Yamamoto, S.1    Hayaishi, O.2
  • 19
    • 0000791513 scopus 로고
    • Catalytic properties and reaction mechanism of indoleamine 2,3-dioxygenase
    • Hayaishi O., Hirata F., Fujiwava M., Ohnishi T., Nukiwa T. Catalytic properties and reaction mechanism of indoleamine 2,3-dioxygenase. FEBS Proc. Meet. 40:1975;131-144.
    • (1975) FEBS Proc. Meet. , vol.40 , pp. 131-144
    • Hayaishi, O.1    Hirata, F.2    Fujiwava, M.3    Ohnishi, T.4    Nukiwa, T.5
  • 20
    • 0141581399 scopus 로고
    • My life with tryptophan - Never a dull moment
    • I. Ishiguro, R. Kido, T. Nagatsy, Y. Nagamura, & Y. Ohta. Toyoake: Fujita Health University Press
    • Hayaishi O. My life with tryptophan - never a dull moment. Ishiguro I., Kido R., Nagatsy T., Nagamura Y., Ohta Y. Advances in Tryptophan Research. 1992;3-16 Fujita Health University Press, Toyoake.
    • (1992) Advances in Tryptophan Research , pp. 3-16
    • Hayaishi, O.1
  • 22
    • 0027419259 scopus 로고
    • Metabolism and function of brain kynurenines
    • Schwarcz R. Metabolism and function of brain kynurenines. Biochem. Soc. Trans. 21:1993;77-82.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 77-82
    • Schwarcz, R.1
  • 23
    • 0027536709 scopus 로고
    • Metabolism and neuropathologic significance of quinolinic acid and kynurenic acid
    • Heyes M.P. Metabolism and neuropathologic significance of quinolinic acid and kynurenic acid. Biochem. Soc. Trans. 21:1993;83-89.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 83-89
    • Heyes, M.P.1
  • 24
    • 0021338289 scopus 로고
    • The excitotoxin quinolinic acid is present and unevenly distributed in the rat brain
    • Moroni F., Lombardi G., Carlà V., Moneti G. The excitotoxin quinolinic acid is present and unevenly distributed in the rat brain. Brain Res. 295:1984;352-355.
    • (1984) Brain Res. , vol.295 , pp. 352-355
    • Moroni, F.1    Lombardi, G.2    Carlà, V.3    Moneti, G.4
  • 28
    • 0035882441 scopus 로고    scopus 로고
    • Enzyme activities involved in tryptophan metabolism along the kynurenine pathway in rabbits
    • Bertazzo A., Ragazzi E., Biasiolo M., Costa C.V.L., Allegri G. Enzyme activities involved in tryptophan metabolism along the kynurenine pathway in rabbits. Biochim. Biophys. Acta. 1527:2001;167-175.
    • (2001) Biochim. Biophys. Acta , vol.1527 , pp. 167-175
    • Bertazzo, A.1    Ragazzi, E.2    Biasiolo, M.3    Costa, C.V.L.4    Allegri, G.5
  • 29
    • 0001333396 scopus 로고
    • A microsomal iron-porphyrin activator of rat liver tryptophan pyrrolase
    • Feigelson P., Greengard O. A microsomal iron-porphyrin activator of rat liver tryptophan pyrrolase. J. Biol. Chem. 236:1961;153-157.
    • (1961) J. Biol. Chem. , vol.236 , pp. 153-157
    • Feigelson, P.1    Greengard, O.2
  • 30
    • 0019362768 scopus 로고
    • Effect of psoralen-induced photodermatitis on tryptophan metabolism in guinea-pigs
    • Allegri G., Costa C., De Antoni A., Baccichetti F., Vanzan S. Effect of psoralen-induced photodermatitis on tryptophan metabolism in guinea-pigs. Farmaco Ed. Sci. 36:1981;557-564.
    • (1981) Farmaco Ed. Sci. , vol.36 , pp. 557-564
    • Allegri, G.1    Costa, C.2    De Antoni, A.3    Baccichetti, F.4    Vanzan, S.5
  • 31
    • 0018148373 scopus 로고
    • Indoleamine 2,3-dioxygenase. Purification and some properties
    • Shimizu T., Nomiyama S., Hirata F., Hayaishi O. Indoleamine 2,3-dioxygenase. Purification and some properties. J. Biol. Chem. 253:1978;4700-4706.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4700-4706
    • Shimizu, T.1    Nomiyama, S.2    Hirata, F.3    Hayaishi, O.4
  • 32
    • 0025894952 scopus 로고
    • Alpha-aminoadipate aminotransferase and kynurenine aminotransferase activities from rat kidney. Evidence for separate identity
    • Mawal M.R., Deshmukh D.R. alpha-aminoadipate aminotransferase and kynurenine aminotransferase activities from rat kidney. Evidence for separate identity. J. Biol. Chem. 266:1991;2573-2575.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2573-2575
    • Mawal, M.R.1    Deshmukh, D.R.2
  • 33
    • 77956995297 scopus 로고
    • Kynurenine hydroxylase
    • Hayaishi O. Kynurenine hydroxylase. Methods Enzymol. 5:1962;807-809.
    • (1962) Methods Enzymol. , vol.5 , pp. 807-809
    • Hayaishi, O.1
  • 34
    • 0000625493 scopus 로고
    • Properties and partial purification of kynureninase
    • Saran A. Properties and partial purification of kynureninase. Biochem. J. 70:1958;182-188.
    • (1958) Biochem. J. , vol.70 , pp. 182-188
    • Saran, A.1
  • 35
    • 0000474008 scopus 로고
    • The kynurenine transaminase of rat kidney
    • Mason M. The kynurenine transaminase of rat kidney. J. Biol. Chem. 211:1954;839-844.
    • (1954) J. Biol. Chem. , vol.211 , pp. 839-844
    • Mason, M.1
  • 36
    • 0000070989 scopus 로고
    • Formation of picolinic and quinolinic acids following enzymatic oxidation of 3-hydroxyanthranilic acid
    • Mehler A.H. Formation of picolinic and quinolinic acids following enzymatic oxidation of 3-hydroxyanthranilic acid. J. Biol. Chem. 218:1956;241-254.
    • (1956) J. Biol. Chem. , vol.218 , pp. 241-254
    • Mehler, A.H.1
  • 37
    • 0017236996 scopus 로고
    • Beef kidney 3-hydroxyanthranilic acid oxygenase. Purification, characterization, and analysis of the assay
    • Koontz W.A., Shiman R. Beef kidney 3-hydroxyanthranilic acid oxygenase. Purification, characterization, and analysis of the assay. J. Biol. Chem. 251:1976;368-377.
    • (1976) J. Biol. Chem. , vol.251 , pp. 368-377
    • Koontz, W.A.1    Shiman, R.2
  • 38
    • 0000936823 scopus 로고
    • Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues II. Enzymatic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid
    • Ichiyama A., Nakamura S., Kawai H., Honjo T., Nishizuka Y., Hayaishi O., Senoh S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues II. Enzymatic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240:1965;740-749.
    • (1965) J. Biol. Chem. , vol.240 , pp. 740-749
    • Ichiyama, A.1    Nakamura, S.2    Kawai, H.3    Honjo, T.4    Nishizuka, Y.5    Hayaishi, O.6    Senoh, S.7
  • 39
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp C., Fridovich I. Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44:1971;276-287.
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 41
  • 42
    • 0014035240 scopus 로고
    • The determination of tryptophan in plasma, liver, and urine
    • Denckla W.D., Dewey H.H. The determination of tryptophan in plasma, liver, and urine. J. Lab. Clin. Med. 69:1967;160-169.
    • (1967) J. Lab. Clin. Med. , vol.69 , pp. 160-169
    • Denckla, W.D.1    Dewey, H.H.2
  • 44
    • 0024595719 scopus 로고
    • Interferon-induced indoleamine 2,3-dioxygenase activity in human mononuclear phagocytes
    • Carlin J.M., Borden E.C., Sondel P.M., Byrne G.I. Interferon-induced indoleamine 2,3-dioxygenase activity in human mononuclear phagocytes. J. Leukocyte Biol. 45:1989;29-34.
    • (1989) J. Leukocyte Biol. , vol.45 , pp. 29-34
    • Carlin, J.M.1    Borden, E.C.2    Sondel, P.M.3    Byrne, G.I.4
  • 45
    • 0016042623 scopus 로고
    • Guinea-pig liver tryptophan pyrrolase. Absence of detectable apoenzyme activity and of hormonal induction by cortisol and possible regulation by tryptophan
    • Badawy.and A.A.-B., Evans M. Guinea-pig liver tryptophan pyrrolase. Absence of detectable apoenzyme activity and of hormonal induction by cortisol and possible regulation by tryptophan. Biochem. J. 138:1974;445-451.
    • (1974) Biochem. J. , vol.138 , pp. 445-451
    • Badawy, A.A.-B.1    Evans, M.2
  • 46
    • 0017170581 scopus 로고
    • Animal liver tryptophan pyrrolases. Absence of apoenzyme and of hormonal induction mechanism from species sensitive to tryptophan toxicity
    • Badawy A.A.-B., Evans M. Animal liver tryptophan pyrrolases. Absence of apoenzyme and of hormonal induction mechanism from species sensitive to tryptophan toxicity. Biochem. J. 158:1976;79-88.
    • (1976) Biochem. J. , vol.158 , pp. 79-88
    • Badawy, A.A.-B.1    Evans, M.2
  • 47
    • 0015526611 scopus 로고
    • Tryptophan pyrrolase in the liver of guinea-pig: The absence of hydrocortisone induction
    • Hvitefelt J., Santti R.S. Tryptophan pyrrolase in the liver of guinea-pig: the absence of hydrocortisone induction. Biochim. Biophys. Acta. 258:1972;358-365.
    • (1972) Biochim. Biophys. Acta , vol.258 , pp. 358-365
    • Hvitefelt, J.1    Santti, R.S.2
  • 48
    • 0014418392 scopus 로고
    • Fish liver tryptophan pyrrolase: The apparent absence of both hormonal and substrate induction
    • Brown J.N., Dodgen C.L. Fish liver tryptophan pyrrolase: the apparent absence of both hormonal and substrate induction. Biochim. Biophys. Acta. 165:1968;463-469.
    • (1968) Biochim. Biophys. Acta , vol.165 , pp. 463-469
    • Brown, J.N.1    Dodgen, C.L.2
  • 49
    • 0013913959 scopus 로고
    • Effect of orally administered tryptophan on tryptophan pyrrolase activity in ovine and bovine
    • Johnson R.J., Dyer L.A. Effect of orally administered tryptophan on tryptophan pyrrolase activity in ovine and bovine. Life Sci. 5:1966;1121-1124.
    • (1966) Life Sci. , vol.5 , pp. 1121-1124
    • Johnson, R.J.1    Dyer, L.A.2
  • 50
    • 0004434793 scopus 로고
    • Tryptophan pyrrolase activity in the liver of adult rana pipiens
    • Spiegel M. Tryptophan pyrrolase activity in the liver of adult rana pipiens. Biol. Bull. 121:1961;547-553.
    • (1961) Biol. Bull. , vol.121 , pp. 547-553
    • Spiegel, M.1
  • 51
    • 0004393077 scopus 로고
    • Control of tryptophan oxygenase and formamidase activity in the gerbil
    • Baughman K.L., Franz J.M. Control of tryptophan oxygenase and formamidase activity in the gerbil. Int. J. Biochem. 2:1971;201-211.
    • (1971) Int. J. Biochem. , vol.2 , pp. 201-211
    • Baughman, K.L.1    Franz, J.M.2
  • 55
    • 0021678429 scopus 로고
    • Metabolites and enzyme activities involved in tryptophan metabolism in two different strains of mouse
    • Costa C., De Antoni A., Baccichetti F., Biasiolo M., Allegri G. Metabolites and enzyme activities involved in tryptophan metabolism in two different strains of mouse. Ital. J. Biochem. 33:1984;319-324.
    • (1984) Ital. J. Biochem. , vol.33 , pp. 319-324
    • Costa, C.1    De Antoni, A.2    Baccichetti, F.3    Biasiolo, M.4    Allegri, G.5
  • 56
    • 0017397028 scopus 로고
    • Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes
    • Taniguchi T., Hirata F., Hayaishi O. Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes. J. Biol. Chem. 252:1977;2774-2776.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2774-2776
    • Taniguchi, T.1    Hirata, F.2    Hayaishi, O.3
  • 57
    • 0020130671 scopus 로고
    • Effect of exposure to light on enzyme activities and tryptophan metabolites of the kynurenine pathway in Wistar, in heterozygous and homozygous adult and newborn Gunn rats
    • Allegri G., Costa C., De Antoni A., Baccichetti F., Vanzan S., Rubaltelli F.F. Effect of exposure to light on enzyme activities and tryptophan metabolites of the kynurenine pathway in Wistar, in heterozygous and homozygous adult and newborn Gunn rats. Photochem Photobiol. 35:1982;691-696.
    • (1982) Photochem Photobiol. , vol.35 , pp. 691-696
    • Allegri, G.1    Costa, C.2    De Antoni, A.3    Baccichetti, F.4    Vanzan, S.5    Rubaltelli, F.F.6
  • 58
    • 0020308552 scopus 로고
    • Strain differences in the tryptophan metabolite excretion and enzyme activities along the kynurenine pathway in rats
    • Costa C., De Antoni A., Baccichetti F., Vanzan S., Appodia M., Allegri G. Strain differences in the tryptophan metabolite excretion and enzyme activities along the kynurenine pathway in rats. Ital. J. Biochem. 31:1982;412-418.
    • (1982) Ital. J. Biochem. , vol.31 , pp. 412-418
    • Costa, C.1    De Antoni, A.2    Baccichetti, F.3    Vanzan, S.4    Appodia, M.5    Allegri, G.6
  • 59
    • 0006144027 scopus 로고
    • Quinolinic metabolism IV. Urinary excretion by man and other mammals as affected by the ingestion of tryptophan
    • Henderson L.M., Ramasarma B.B., Johnson B.C. Quinolinic metabolism IV. Urinary excretion by man and other mammals as affected by the ingestion of tryptophan. J. Biol. Chem. 181:1949;731-738.
    • (1949) J. Biol. Chem. , vol.181 , pp. 731-738
    • Henderson, L.M.1    Ramasarma, B.B.2    Johnson, B.C.3


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