L-cysteine metabolism in guinea pig and rat tissues

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 116, Issue 2, 1997, Pages 223-226

  Wrobel M ^a,b   Ubuka, T ^a   Yao, W B ^a   Abe, T ^a  

^a OKAYAMA UNIVERSITY MEDICAL SCHOOL   (Japan)

^b JAGIELLONIAN UNIVERSITY MEDICAL COLLEGE   (Poland)

Author keywords

3 mercaptolactate cysteine disulfide; 3 mercaptopyruvate sulfurtransferase; guinea pig; rat; rhodanese; sulfane sulfur; cystathionase

Indexed keywords

CYSTATHIONINE GAMMA LYASE; THIOSULFATE SULFURTRANSFERASE;

ANIMAL TISSUE; ARTICLE; BRAIN; CONTROLLED STUDY; ENZYME ACTIVITY; GUINEA PIG; KIDNEY; LIVER METABOLISM; MALE; NONHUMAN; PRIORITY JOURNAL; RAT; SPECIES DIFFERENCE;

EID: 0030894008     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(96)00216-7     Document Type: Article

References (17)

1. Abdolrasulnia, R.; Wood, J.L. Biochemistry of thiocystine. In: Cavallini, D.; Gaull, G.E.; Zappia, V. (eds). Natural Sulfur Compounds. New York: Plenum Press; 1980:483-491.
2. Cooper, A.J.L. Biochemistry of sulfur-containing amino-acids. Annu. Rev. Biochem. 52:187-222;1986.
3. Hosaki, Y.; Nishina, H.; Ubuka, T. Metabolism of L-cysteine in guinea pig liver. Acta Med. Okayama 40(1):11-15;1986.
4. Kato, A.; Ogura, H.; Kimura, T.; Kawai, T.; Suda, M. Control mechanism in the rat liver enzyme system converting L-methionine to L-cysteine. II. Crystallization of the serine dehydratase inhibitor-forming enzyme and its identity with cystathionase, homoserine dehydratase, cysteine desulfhydrase. J. Biochem. 59:34-39;1966.
5. Kobayashi, K. Studies on the new metabolites of cystine: I. Orientation studies on the in vitro formation of S-(carboxyethylthio) cysteine and S-(2-hydroxy-2-carboxyethylthio) cysteine from cystine and its related compounds. Physiol. Chem. Phys. 2:455-456;1970.
6. Kun, E. The reaction of β-mercapyopyruvate with lactic dehydrogenase of heart muscle. Biochem. Biophys. Acta 25:135-137;1957.
7. Matsuo, Y.; Greenberg, D.M. A crystalline enzyme that cleaves homoserine and cystathionine. J. Biol. Chem. 230: 545-560;1958.
8. Sörbo, B. Rhodanese. In: Colowick, S.P.; Kaplan, N.O. (eds). Methods in Enzymology, Vol. 2. New York: Academic Press; 1955:334-337.
9. Stipanuk, M.H. Metabolism of sulfur-containing amino acids. Annu. Rev. Nutr. 6:179-209;1986.
10. Szczepkowski, T.W.; Wood, J.L. The cystathionase-rhodanese system. Biochem. Biophys. Acta 139;469-478;1967.
11. Ubuka, T.; Akagi, R.; Kiguchi, S.; Taniguchi, M.; Mikami, H. Biosynthesis of S-(2-hydroxy-2-carboxyethylthio-)-L-cysteine (3-mercaptolactate-cysteine disulfide) by the rat heart. Biochem. Int. 6:291-296;1983.
12. Ubuka, T.; Hosaki, Y.; Nishina, H.; Ikeda, T. 3-Mercaptopyruvate sulfurtransferase activity in guinea pig and rat tissue. Physiol. Chem. Phys. 17:41-43;1985.
13. Ubuka, T.; Ohta, J.; Akagi, R.; Hosaki, Y.; Ishimoto, Y.; Kiguchi, S.; Ikeda T.; Ishino, K. Metabolism of L-cysteine via transamination pathway (3-mercaptopyruvate pathway). Amino Acids 3:243-252;1992.
14. Valentine, W.N.; Frankenfeld, J.K. 3-Mercaptopyruvate sulfurtransferase (EC 2.8.1.2): A simple assay adapted to human blood cells. Clin. Chim. Acta 51:205-210;1974.
15. Westley, J. Rhodanese and the sulfane pool. In: Enzymatic basis of detoxification. New York: Academic Press; 1980:245-262.
16. Wood, L. Sulfane sulfur. In: Jakoby, W.B.; Griffith, O.W. (eds). Methods in Enzymology, Vol. 143. San Diego: Academic Press; 1987:25-29.
17. Yamaguchi, K.; Hosokawa, Y.; Kohashi, N.; Kori, Y.; Sakakibara, S.; Ueda, I. Rat liver cysteine dioxygenase (cysteine oxidase). J. Biochem. 8:3479-3491;1978.