메뉴 건너뛰기




Volumn 1764, Issue 5, 2006, Pages 961-971

Enzymatic and biochemical properties of a novel human serine dehydratase isoform

Author keywords

Isoform; Recombinant protein; Serine dehydratase; Translational efficiency

Indexed keywords

COMPLEMENTARY DNA; ISOENZYME; LEUCINE; LIVER ENZYME; MESSENGER RNA; PROLINE; PYRIDOXAL 5 PHOSPHATE; RECOMBINANT ENZYME; SERINE DEHYDRATASE; THREONINE DEHYDRATASE; VALINE;

EID: 33646504092     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.02.010     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 0006414976 scopus 로고    scopus 로고
    • Structure and function relationships of serine dehydratases from various sources
    • Ogawa H. Structure and function relationships of serine dehydratases from various sources. Trends Comp. Biochem. Physiol. 6 (2000) 1-19
    • (2000) Trends Comp. Biochem. Physiol. , vol.6 , pp. 1-19
    • Ogawa, H.1
  • 3
    • 0014597374 scopus 로고
    • The properties of crystalline serine dehydratase of rat liver
    • Nakagawa H., and Kimura H. The properties of crystalline serine dehydratase of rat liver. J. Biochem. 66 (1969) 669-683
    • (1969) J. Biochem. , vol.66 , pp. 669-683
    • Nakagawa, H.1    Kimura, H.2
  • 4
    • 0015239397 scopus 로고
    • Studies on the induction and repression of enzymes in rat liver: VI. Some properties and the metabolic regulation of two isozymic forms of serine dehydratase
    • Inoue H., Kasper C., and Pitot H.C. Studies on the induction and repression of enzymes in rat liver: VI. Some properties and the metabolic regulation of two isozymic forms of serine dehydratase. J. Biol. Chem. 246 (1971) 2626-2632
    • (1971) J. Biol. Chem. , vol.246 , pp. 2626-2632
    • Inoue, H.1    Kasper, C.2    Pitot, H.C.3
  • 8
    • 14144252024 scopus 로고    scopus 로고
    • Crystal structure of the pyrodxal-5′-phosphate-dependent serine dehydratase from human liver
    • Sun L., Bartlam M., Liu Y., Pang H., and Rao Z. Crystal structure of the pyrodxal-5′-phosphate-dependent serine dehydratase from human liver. Protein Sci. 14 (2005) 791-798
    • (2005) Protein Sci. , vol.14 , pp. 791-798
    • Sun, L.1    Bartlam, M.2    Liu, Y.3    Pang, H.4    Rao, Z.5
  • 10
    • 0015937406 scopus 로고
    • The glycine cleavage system. Comparison, reaction mechanism, and physiological significance
    • Kikuchi G. The glycine cleavage system. Comparison, reaction mechanism, and physiological significance. Mol. Cell. Biochem. 1 (1973) 179-203
    • (1973) Mol. Cell. Biochem. , vol.1 , pp. 179-203
    • Kikuchi, G.1
  • 11
    • 0033522908 scopus 로고    scopus 로고
    • Flux of the l-serine metabolism in rat liver. The predominant contribution of serine dehydratase
    • Xue H.H., Fujie M., Sakgauchi T., Oda T., Ogawa H., Kneer N.M., Lardy H.A., and Ichiyama A. Flux of the l-serine metabolism in rat liver. The predominant contribution of serine dehydratase. J. Biol. Chem. 274 (1999) 16020-16027
    • (1999) J. Biol. Chem. , vol.274 , pp. 16020-16027
    • Xue, H.H.1    Fujie, M.2    Sakgauchi, T.3    Oda, T.4    Ogawa, H.5    Kneer, N.M.6    Lardy, H.A.7    Ichiyama, A.8
  • 12
    • 0016609161 scopus 로고
    • Immunohistochemical demonstration of serine dehydratase in rat liver
    • Kitagawa T., and Pitot H.C. Immunohistochemical demonstration of serine dehydratase in rat liver. Am. J. Pathol. 78 (1975) 309-318
    • (1975) Am. J. Pathol. , vol.78 , pp. 309-318
    • Kitagawa, T.1    Pitot, H.C.2
  • 13
    • 0029001857 scopus 로고
    • Periportal expression of the serine dehydratase gene in rat liver
    • Ogawa H., and Kawamata S. Periportal expression of the serine dehydratase gene in rat liver. Histochem. J. 27 (1995) 380-387
    • (1995) Histochem. J. , vol.27 , pp. 380-387
    • Ogawa, H.1    Kawamata, S.2
  • 15
    • 0033523088 scopus 로고    scopus 로고
    • Flux of l-serine metabolism in rabbit, human, and dog livers: substantial contributions of both mitochondrial and peroxisomal serine pyruvate/alanine:glyoxylate aminotransferase
    • Xue H.H., Sakaguchi T., Fujie M., Ogawa H., and Ichiyama A. Flux of l-serine metabolism in rabbit, human, and dog livers: substantial contributions of both mitochondrial and peroxisomal serine pyruvate/alanine:glyoxylate aminotransferase. J. Biol. Chem. 274 (1999) 16028-16033
    • (1999) J. Biol. Chem. , vol.274 , pp. 16028-16033
    • Xue, H.H.1    Sakaguchi, T.2    Fujie, M.3    Ogawa, H.4    Ichiyama, A.5
  • 16
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 17
    • 0030694458 scopus 로고    scopus 로고
    • Recombinant expression of rat glycine N-methyltransferase and evidence for contribution of N-terminal acetylation to co-operative binding of S-adenosylmethionine
    • Ogawa H., Gomi T., Takata Y., Date T., and Fujioka M. Recombinant expression of rat glycine N-methyltransferase and evidence for contribution of N-terminal acetylation to co-operative binding of S-adenosylmethionine. Biochem. J. 327 (1997) 407-412
    • (1997) Biochem. J. , vol.327 , pp. 407-412
    • Ogawa, H.1    Gomi, T.2    Takata, Y.3    Date, T.4    Fujioka, M.5
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemli, U.K.1
  • 21
    • 0021191196 scopus 로고
    • Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
    • Snell K. Enzymes of serine metabolism in normal, developing and neoplastic rat tissues. Adv. Enzyme Regul. 22 (1984) 325-400
    • (1984) Adv. Enzyme Regul. , vol.22 , pp. 325-400
    • Snell, K.1
  • 22
    • 0000908762 scopus 로고    scopus 로고
    • Neidhardt F., CurtissIII R., Ingraham J., Lin E., Low B., Magasanik B., Bezniloff W., Riley M., Schaechter M., and Umbarger H. (Eds), American Society for Microbiology, Washington, DC
    • Henaut A., and Danchin A. In: Neidhardt F., CurtissIII R., Ingraham J., Lin E., Low B., Magasanik B., Bezniloff W., Riley M., Schaechter M., and Umbarger H. (Eds). Escherichia coli and Salmonella typhimurium cellular and molecular biology vol. 2 (1996), American Society for Microbiology, Washington, DC 2047-2066
    • (1996) Escherichia coli and Salmonella typhimurium cellular and molecular biology , vol.2 , pp. 2047-2066
    • Henaut, A.1    Danchin, A.2
  • 23
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31 (2003) 3406-3415
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 24
    • 25444506890 scopus 로고    scopus 로고
    • Mice have a transcribed l-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene
    • Edgar A.J. Mice have a transcribed l-threonine aldolase/GLY1 gene, but the human GLY1 gene is a non-processed pseudogene. BMC Genomics 6 (2005) 32
    • (2005) BMC Genomics , vol.6 , pp. 32
    • Edgar, A.J.1
  • 25
    • 0025082519 scopus 로고
    • Nutritional regulation and tissue-specific expression of the serine dehydratase gene in rat
    • Ogawa H., Fujioka M., Date T., Mueckler M., Su Y., and Pitot H.C. Nutritional regulation and tissue-specific expression of the serine dehydratase gene in rat. J. Biol. Chem. 265 (1990) 14407-14413
    • (1990) J. Biol. Chem. , vol.265 , pp. 14407-14413
    • Ogawa, H.1    Fujioka, M.2    Date, T.3    Mueckler, M.4    Su, Y.5    Pitot, H.C.6
  • 26
    • 0036136732 scopus 로고    scopus 로고
    • S-Adenosylmethionine. A control switch that regulates liver function
    • Mato J.M., Corrales F.J., Lu S.C., and Avila M.A. S-Adenosylmethionine. A control switch that regulates liver function. FASEB J. 16 (2002) 15-26
    • (2002) FASEB J. , vol.16 , pp. 15-26
    • Mato, J.M.1    Corrales, F.J.2    Lu, S.C.3    Avila, M.A.4
  • 27
    • 0346991731 scopus 로고    scopus 로고
    • Induction of human methionine adenosyltransferase 2A expression by tumor necrosis factor alpha. Role of NF-kappaB and AP-1
    • Yang H., Sadda M.R., Yu V., Zeng Y., Lee T.D., Ou X., Chen L., and Lu S.C. Induction of human methionine adenosyltransferase 2A expression by tumor necrosis factor alpha. Role of NF-kappaB and AP-1. J. Biol. Chem. 278 (2003) 50887-50896
    • (2003) J. Biol. Chem. , vol.278 , pp. 50887-50896
    • Yang, H.1    Sadda, M.R.2    Yu, V.3    Zeng, Y.4    Lee, T.D.5    Ou, X.6    Chen, L.7    Lu, S.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.