메뉴 건너뛰기




Volumn 32, Issue 4, 2000, Pages 405-416

Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase - A potential target for cancer chemotherapy

Author keywords

Catalysis; Chemotherapeutic target; Drug design; Inhibitors; PLP; SHMT; X ray structure

Indexed keywords

AMINO ACID; GLYCINE HYDROXYMETHYLTRANSFERASE; SERINE;

EID: 0034174531     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00126-0     Document Type: Article
Times cited : (40)

References (60)
  • 1
    • 0012996147 scopus 로고
    • The biochemistry of folic acid and related pteridines
    • Blakely R.L. The biochemistry of folic acid and related pteridines. Frontiers in Biology. 13:1969;189-218.
    • (1969) Frontiers in Biology , vol.13 , pp. 189-218
    • Blakely, R.L.1
  • 4
    • 0031843013 scopus 로고    scopus 로고
    • Multidrug resistance and its reversal
    • Volm M. Multidrug resistance and its reversal. Anticancer Research. 184:1998;2905-2917.
    • (1998) Anticancer Research , vol.184 , pp. 2905-2917
    • Volm, M.1
  • 5
    • 1442336560 scopus 로고
    • Co-operative interactions of tetrahydrofolate with purified pig kidney serine transhydroxymethylase and loss of this co-operativity in L1210 tumors and in mice bearing these tumors
    • Harish Kumar P.M., North T.A., Mangum J., Appaji Rao N. Co-operative interactions of tetrahydrofolate with purified pig kidney serine transhydroxymethylase and loss of this co-operativity in L1210 tumors and in mice bearing these tumors. Proceedings of the National Academy of Science (USA). 73:1976;1950-1953.
    • (1976) Proceedings of the National Academy of Science (USA) , vol.73 , pp. 1950-1953
    • Harish Kumar, P.M.1    North, T.A.2    Mangum, J.3    Appaji Rao, N.4
  • 6
    • 0002725079 scopus 로고
    • in: T. Ozawa (Ed.) Japan Scientific Society Press, Tokyo, Springer-Verlag, Berlin
    • N. Appaji Rao, in: T. Ozawa (Ed.), New Trends in Biological Chemistry, Japan Scientific Society Press, Tokyo, Springer-Verlag, Berlin, 1991, pp. 333-340.
    • (1991) New Trends in Biological Chemistry , pp. 333-340
    • N. Appaji Rao1
  • 7
    • 0032530853 scopus 로고    scopus 로고
    • The crystal structure of human cytosolic serine hydroxymethyltransferase: A target for cancer chemotherapy
    • Renwick S.B., Snell K., Baumann U. The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure. 6:1998;1105-1116.
    • (1998) Structure , vol.6 , pp. 1105-1116
    • Renwick, S.B.1    Snell, K.2    Baumann, U.3
  • 8
    • 0031873380 scopus 로고    scopus 로고
    • Cobalamine-dependent methionine synthase and serine hydroxymethyltransferase: Targets for chemotherapeutic intervention?
    • Matthews R.G., Drummond J.T., Webb H.K. Cobalamine-dependent methionine synthase and serine hydroxymethyltransferase: targets for chemotherapeutic intervention? Advances in Enzyme Regulation. 38:1998;377-392.
    • (1998) Advances in Enzyme Regulation , vol.38 , pp. 377-392
    • Matthews, R.G.1    Drummond, J.T.2    Webb, H.K.3
  • 9
    • 0030862155 scopus 로고    scopus 로고
    • Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in de novo purine synthesis in Saccharomyces cerevisiae
    • Kastanos E.K., Woldman Y.V., Appling D.R. Role of mitochondrial and cytoplasmic serine hydroxymethyltransferase isozymes in de novo purine synthesis in Saccharomyces cerevisiae. Biochemistry. 36:1997;14956-14964.
    • (1997) Biochemistry , vol.36 , pp. 14956-14964
    • Kastanos, E.K.1    Woldman, Y.V.2    Appling, D.R.3
  • 10
    • 0024601238 scopus 로고
    • Effects of a triazine antifolate (NSC 127755) on SHMT in myeloma cells in culture
    • Snell K., Riches D. Effects of a triazine antifolate (NSC 127755) on SHMT in myeloma cells in culture. Cancer Letters. 44:1989;217-220.
    • (1989) Cancer Letters , vol.44 , pp. 217-220
    • Snell, K.1    Riches, D.2
  • 11
    • 0026063520 scopus 로고
    • 5-formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase
    • Stover P., Schirch V. 5-formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase. Journal of Biological Chemistry. 266:1991;1543-1550.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 1543-1550
    • Stover, P.1    Schirch, V.2
  • 12
    • 0017537125 scopus 로고
    • Effect of diketopiperazine on mouse liver regeneration following hepatectomy
    • Sergeev A.V. Effect of diketopiperazine on mouse liver regeneration following hepatectomy. Vopr. Med. Khim. 23:1977;601-606.
    • (1977) Vopr. Med. Khim. , vol.23 , pp. 601-606
    • Sergeev, A.V.1
  • 13
    • 0021772473 scopus 로고
    • Kinetic mechanism of the interaction of D-cycloserine with serine hydroxymethyltransferase
    • Manohar R., Appu Rao A.G., Appaji Rao N. Kinetic mechanism of the interaction of D-cycloserine with serine hydroxymethyltransferase. Biochemistry. 23:1984;4116-4122.
    • (1984) Biochemistry , vol.23 , pp. 4116-4122
    • Manohar, R.1    Appu Rao, A.G.2    Appaji Rao, N.3
  • 15
    • 0026235523 scopus 로고
    • Interactions of methoxyamine with pyridoxal-5′-phosphate-Schiff's base at the active site of sheep liver serine hydroxymethyltransferase
    • Acharya J.K., Prakash V., Appu Rao A.G., Savithri H.S., Appaji Rao N. Interactions of methoxyamine with pyridoxal-5′-phosphate-Schiff's base at the active site of sheep liver serine hydroxymethyltransferase. Indian Journal of Biochemistry and Biophysics. 28:1991;381-388.
    • (1991) Indian Journal of Biochemistry and Biophysics , vol.28 , pp. 381-388
    • Acharya, J.K.1    Prakash, V.2    Appu Rao, A.G.3    Savithri, H.S.4    Appaji Rao, N.5
  • 16
    • 0026775163 scopus 로고
    • A novel intermediate in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase
    • Acharya J.K., Appaji Rao N. A novel intermediate in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase. Journal of Biological Chemistry. 267:1992;19066-19071.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 19066-19071
    • Acharya, J.K.1    Appaji Rao, N.2
  • 18
    • 0020539802 scopus 로고
    • Characterization of the E. coli gene for SHMT
    • Plamann M.D., Stauffer G.V. Characterization of the E. coli gene for SHMT. Gene. 22:1983;9-18.
    • (1983) Gene , vol.22 , pp. 9-18
    • Plamann, M.D.1    Stauffer, G.V.2
  • 21
    • 0031035739 scopus 로고    scopus 로고
    • Molecular cloning, characterization and regulation of the human mitochondrial serine hydroxymethyltransferase gene
    • Stover P., Chen L., Suh J.R., Stover D., Keyomarsi K., Shane B. Molecular cloning, characterization and regulation of the human mitochondrial serine hydroxymethyltransferase gene. Journal of Biological Chemistry. 272:1997;1842-1848.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 1842-1848
    • Stover, P.1    Chen, L.2    Suh, J.R.3    Stover, D.4    Keyomarsi, K.5    Shane, B.6
  • 22
    • 0032515921 scopus 로고    scopus 로고
    • Molecular cloning, characterization and alternate splicing of the human cytoplasmic serine hydroxymethyltransferase gene
    • Girgis S., Ilya M., Nasrallah J.R.S., Oppenheim E., Zanetti K.A., Mastri M.G., Stover P.J. Molecular cloning, characterization and alternate splicing of the human cytoplasmic serine hydroxymethyltransferase gene. Gene. 210:1998;315-324.
    • (1998) Gene , vol.210 , pp. 315-324
    • Girgis, S.1    Ilya, M.2    Nasrallah, J.R.S.3    Oppenheim, E.4    Zanetti, K.A.5    Mastri, M.G.6    Stover, P.J.7
  • 23
    • 0014428379 scopus 로고
    • Studies on serine hydroxymethylase isozymes from rat liver
    • Nakano Y., Fujioka M., Wada H. Studies on serine hydroxymethylase isozymes from rat liver. Biochimica Biophysica Acta. 159:1968;19-26.
    • (1968) Biochimica Biophysica Acta , vol.159 , pp. 19-26
    • Nakano, Y.1    Fujioka, M.2    Wada, H.3
  • 24
    • 0030603220 scopus 로고    scopus 로고
    • Isolation of retinoic acid-repressed genes from P19 embryonal carcinoma cells
    • Nakshatri H., Bouillet P., Bhat-Nakshatri P., Chambon P. Isolation of retinoic acid-repressed genes from P19 embryonal carcinoma cells. Gene. 174:1996;79-84.
    • (1996) Gene , vol.174 , pp. 79-84
    • Nakshatri, H.1    Bouillet, P.2    Bhat-Nakshatri, P.3    Chambon, P.4
  • 26
    • 0028084927 scopus 로고
    • The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and analysis of the evolutionary relationships among SHMTs
    • Usha R., Savithri H.S., Appaji Rao N. The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and analysis of the evolutionary relationships among SHMTs. Biochimica Biophysica Acta. 1204:1994;75-83.
    • (1994) Biochimica Biophysica Acta , vol.1204 , pp. 75-83
    • Usha, R.1    Savithri, H.S.2    Appaji Rao, N.3
  • 27
    • 0028044574 scopus 로고
    • Evolutionary relationships among PLP-dependent enzymes: Regio-specific α, β and γ families
    • Alexander F.W., Sandmeier E., Mehta P.K., Christen P. Evolutionary relationships among PLP-dependent enzymes: regio-specific α, β and γ families. European Journal of Biochemistry. 219:1994;953-960.
    • (1994) European Journal of Biochemistry , vol.219 , pp. 953-960
    • Alexander, F.W.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4
  • 28
    • 0013902457 scopus 로고
    • Conformation and reaction specificity in pyridoxal-5′-phosphate enzymes
    • Dunathan H.C. Conformation and reaction specificity in pyridoxal-5′-phosphate enzymes. Proceedings of the National Academy of Science (USA). 55:1966;712-716.
    • (1966) Proceedings of the National Academy of Science (USA) , vol.55 , pp. 712-716
    • Dunathan, H.C.1
  • 30
    • 0028033730 scopus 로고
    • Interactions of L-serine at the active site of serine hydroxymethyltransferase: Induction of thermal stability
    • Bhaskar B., Prakash V., Savithri H.S., Appaji Rao N. Interactions of L-serine at the active site of serine hydroxymethyltransferase: induction of thermal stability. Biochimica Biophysica Acta. 1209:1994;40-50.
    • (1994) Biochimica Biophysica Acta , vol.1209 , pp. 40-50
    • Bhaskar, B.1    Prakash, V.2    Savithri, H.S.3    Appaji Rao, N.4
  • 31
    • 0029095080 scopus 로고
    • The affinity of pyridoxal-5′-phosphate for folding intermediates of Escherichia coli serine hydroxymethyltransferase
    • Cai K., Schirch V. The affinity of pyridoxal-5′-phosphate for folding intermediates of Escherichia coli serine hydroxymethyltransferase. Journal of Biological Chemistry. 270:1995;18252-18259.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 18252-18259
    • Cai, K.1    Schirch, V.2
  • 32
    • 0030019662 scopus 로고    scopus 로고
    • Structural studies on the folding intermediates of serine hydroxymethyltransferase using single tryptophan mutants
    • Cai K., Schirch V. Structural studies on the folding intermediates of serine hydroxymethyltransferase using single tryptophan mutants. Journal of Biological Chemistry. 271:1996;2987-2994.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 2987-2994
    • Cai, K.1    Schirch, V.2
  • 33
    • 0029910143 scopus 로고    scopus 로고
    • Structural studies on the folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer
    • Cai K., Schirch V. Structural studies on the folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer. Journal of Biological Chemistry. 271:1996;27311-27320.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 27311-27320
    • Cai, K.1    Schirch, V.2
  • 35
    • 0032931341 scopus 로고    scopus 로고
    • Guanidine hydrochloride induced reversible unfolding of sheep liver serine hydroxymethyltransferase
    • Venkatesha B., Udgaonkar J.B., Appaji Rao N., Savithri H.S. Guanidine hydrochloride induced reversible unfolding of sheep liver serine hydroxymethyltransferase. Journal of Bioscience. 24:1999;101-109.
    • (1999) Journal of Bioscience , vol.24 , pp. 101-109
    • Venkatesha, B.1    Udgaonkar, J.B.2    Appaji Rao, N.3    Savithri, H.S.4
  • 37
    • 0021336358 scopus 로고
    • Cloning and characterization of the gene for Salmonella typhimurium serine hydroxymethyltransferase
    • Urbanowski M.L., Plamann M.D., Stauffer L.T., Stauffer G.V. Cloning and characterization of the gene for Salmonella typhimurium serine hydroxymethyltransferase. Gene. 27:1984;47-54.
    • (1984) Gene , vol.27 , pp. 47-54
    • Urbanowski, M.L.1    Plamann, M.D.2    Stauffer, L.T.3    Stauffer, G.V.4
  • 38
    • 0025818869 scopus 로고
    • Complete sequence of the Campylobacter jejuni gly A gene encoding serine hydroxymethyltransferase
    • Chan V.L., Bingham H.L. Complete sequence of the Campylobacter jejuni gly A gene encoding serine hydroxymethyltransferase. Gene. 101:1991;51-58.
    • (1991) Gene , vol.101 , pp. 51-58
    • Chan, V.L.1    Bingham, H.L.2
  • 39
    • 0026533305 scopus 로고
    • Characterization of the formate (for) locus, which encodes the cytosolic serine hydroxymethyltransferase of Neurospora crassa
    • McClung C.R., Davis C.R., Page K.M., Denome S.A. Characterization of the formate (for) locus, which encodes the cytosolic serine hydroxymethyltransferase of Neurospora crassa. Molecular and Cellular Biology. 12:1992;1412-1421.
    • (1992) Molecular and Cellular Biology , vol.12 , pp. 1412-1421
    • McClung, C.R.1    Davis, C.R.2    Page, K.M.3    Denome, S.A.4
  • 40
    • 0027414462 scopus 로고
    • Molecular cloning and expression of the gene for serine hydroxymethyltransferase from an obligate methylotroph Hyphomicrobium methylovorum GM2
    • Atsuro M., Toyokazu Y., Kenji Y., Chieko Y., Tadashi T., Hiroyuki T., Toshio M., Yoshikazu I. Molecular cloning and expression of the gene for serine hydroxymethyltransferase from an obligate methylotroph Hyphomicrobium methylovorum GM2. European Journal of Biochemistry. 212:1993;745-750.
    • (1993) European Journal of Biochemistry , vol.212 , pp. 745-750
    • Atsuro, M.1    Toyokazu, Y.2    Kenji, Y.3    Chieko, Y.4    Tadashi, T.5    Hiroyuki, T.6    Toshio, M.7    Yoshikazu, I.8
  • 41
    • 0026669442 scopus 로고
    • Nucleotide sequence and expression of cDNA encoding rabbit liver cytosolic serine hydroxymethyltransferase
    • Byrne P.C., Sanders P.G., Snell K. Nucleotide sequence and expression of cDNA encoding rabbit liver cytosolic serine hydroxymethyltransferase. Biochemical Journal. 286:1992;117-123.
    • (1992) Biochemical Journal , vol.286 , pp. 117-123
    • Byrne, P.C.1    Sanders, P.G.2    Snell, K.3
  • 42
    • 0026766649 scopus 로고
    • Identification and localization of multiple forms of serine hydroxymethyltransferase in pea (Pisum sativum) and characterization of a cDNA encoding a mitochondrial isoform
    • Turner S.R., Ireland R., Morgan C., Rawsthorne S. Identification and localization of multiple forms of serine hydroxymethyltransferase in pea (Pisum sativum) and characterization of a cDNA encoding a mitochondrial isoform. Journal of Biological Chemistry. 267:1992;13528-13534.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 13528-13534
    • Turner, S.R.1    Ireland, R.2    Morgan, C.3    Rawsthorne, S.4
  • 43
    • 0028206255 scopus 로고
    • Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine
    • McNeil J.B., McIntosh E.M., Taylor B.V., Zhang F., Tang S., Bognar A.L. Cloning and molecular characterization of three genes, including two genes encoding serine hydroxymethyltransferases, whose inactivation is required to render yeast auxotrophic for glycine. Journal of Biological Chemistry. 269:1994;9155-9165.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 9155-9165
    • McNeil, J.B.1    McIntosh, E.M.2    Taylor, B.V.3    Zhang, F.4    Tang, S.5    Bognar, A.L.6
  • 44
    • 0029013974 scopus 로고
    • CDNA cloning, overexpression in E. coli, purification and characterization of sheep liver cytosolic serine hydroxymethyltransferase
    • Jagath-Reddy J., Ganesan K., Savithri H.S., Datta A., Appaji Rao N. cDNA cloning, overexpression in E. coli, purification and characterization of sheep liver cytosolic serine hydroxymethyltransferase. European Journal of Biochemistry. 230:1995;533-537.
    • (1995) European Journal of Biochemistry , vol.230 , pp. 533-537
    • Jagath-Reddy, J.1    Ganesan, K.2    Savithri, H.S.3    Datta, A.4    Appaji Rao, N.5
  • 45
    • 0021881054 scopus 로고
    • Serine hydroxymethyltransferase from Escherichia coli: Purification and properties
    • Schirch V., Hopkins S., Villar E., Angelaccio S. Serine hydroxymethyltransferase from Escherichia coli: purification and properties. Journal of Bacteriology. 163:1985;1-7.
    • (1985) Journal of Bacteriology , vol.163 , pp. 1-7
    • Schirch, V.1    Hopkins, S.2    Villar, E.3    Angelaccio, S.4
  • 47
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package (version 3.2)
    • Felsentein J. PHYLIP - Phylogeny inference package (version 3.2). Cladistics. 5:1989;164.
    • (1989) Cladistics , vol.5 , pp. 164
    • Felsentein, J.1
  • 48
    • 0030857353 scopus 로고    scopus 로고
    • Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase
    • Jagath J.R., Sharma B., Bhaskar B., Datta A., Appaji Rao N., Savithri H.S. Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase. European Journal of Biochemistry. 247:1997;372-379.
    • (1997) European Journal of Biochemistry , vol.247 , pp. 372-379
    • Jagath, J.R.1    Sharma, B.2    Bhaskar, B.3    Datta, A.4    Appaji Rao, N.5    Savithri, H.S.6
  • 49
    • 0026788143 scopus 로고
    • Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase
    • Usha R., Savithri H.S., Appaji Rao N. Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase. Journal of Biological Chemistry. 267:1992;9289-9293.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 9289-9293
    • Usha, R.1    Savithri, H.S.2    Appaji Rao, N.3
  • 51
    • 0031324389 scopus 로고    scopus 로고
    • The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase
    • Talwar R., Jagath J.R., Datta A., Prakash V., Savithri H.S., Appaji Rao N. The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase. Acta Biochimica Polonica. 44:1997;679-688.
    • (1997) Acta Biochimica Polonica , vol.44 , pp. 679-688
    • Talwar, R.1    Jagath, J.R.2    Datta, A.3    Prakash, V.4    Savithri, H.S.5    Appaji Rao, N.6
  • 52
    • 0030800643 scopus 로고    scopus 로고
    • The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase
    • Jagath J.R., Sharma B., Appaji Rao N., Savithri H.S. The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. Journal of Biological Chemistry. 272:1997;24355-24362.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 24355-24362
    • Jagath, J.R.1    Sharma, B.2    Appaji Rao, N.3    Savithri, H.S.4
  • 53
    • 0031709347 scopus 로고    scopus 로고
    • The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis
    • Pascarella S., Angelaccio S., Contestabile R., Fratte S.D., DiSalvo M., Bossa F. The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis. Protein Science. 7:1998;1976-1982.
    • (1998) Protein Science , vol.7 , pp. 1976-1982
    • Pascarella, S.1    Angelaccio, S.2    Contestabile, R.3    Fratte, S.D.4    DiSalvo, M.5    Bossa, F.6
  • 54
    • 0026599430 scopus 로고
    • Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites
    • Poulin R., Lu L., Ackermann B., Bey P., Pegg A.E. Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by alpha-difluoromethylornithine. Characterization of sequences at the inhibitor and coenzyme binding sites. Journal of Biological Chemistry. 267:1992;150-158.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 150-158
    • Poulin, R.1    Lu, L.2    Ackermann, B.3    Bey, P.4    Pegg, A.E.5
  • 55
    • 0024522515 scopus 로고
    • The β-subunit of tryptophan synthase: Clarification of the roles of His 86, Lys 87, Arg 148, Cys 170 and Cys 230
    • Miles E.W., Kawasaki H., Ahmed S.A., Morita H., Nagata S. The β-subunit of tryptophan synthase: clarification of the roles of His 86, Lys 87, Arg 148, Cys 170 and Cys 230. Journal of Biological Chemistry. 264:1989;6280-6287.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 6280-6287
    • Miles, E.W.1    Kawasaki, H.2    Ahmed, S.A.3    Morita, H.4    Nagata, S.5
  • 56
    • 0032575276 scopus 로고    scopus 로고
    • The effect of His-228 on the catalytic efficiency and stereospecificity of the serine hydroxymethyltransferase catalyzed exchange of the alpha-protons of amino acids
    • Fitzpatrick T.B., Malthouse P.G. The effect of His-228 on the catalytic efficiency and stereospecificity of the serine hydroxymethyltransferase catalyzed exchange of the alpha-protons of amino acids. Biochimica Biophysica Acta. 1386:1998;220-226.
    • (1998) Biochimica Biophysica Acta , vol.1386 , pp. 220-226
    • Fitzpatrick, T.B.1    Malthouse, P.G.2
  • 58
    • 0028040757 scopus 로고
    • The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase
    • Fratte S.D., Iurescia S., Angelaccio S., Bossa F., Schirch V. The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase. European Journal of Biochemistry. 225:1994;395-401.
    • (1994) European Journal of Biochemistry , vol.225 , pp. 395-401
    • Fratte, S.D.1    Iurescia, S.2    Angelaccio, S.3    Bossa, F.4    Schirch, V.5
  • 59
    • 0030660382 scopus 로고    scopus 로고
    • Role of R-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group
    • Jagath J.R., Appaji Rao N., Savithri H.S. Role of R-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group. Biochemical Journal. 327:1997;877-882.
    • (1997) Biochemical Journal , vol.327 , pp. 877-882
    • Jagath, J.R.1    Appaji Rao, N.2    Savithri, H.S.3
  • 60
    • 0033614832 scopus 로고    scopus 로고
    • Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8Å resolution: Mechanistic implications
    • Scarsdale J.N., Kazarina G., Radaev S., Schirch V., Wright H.T. Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8Å resolution: mechanistic implications. Biochemistry. 38:1999;8347-8358.
    • (1999) Biochemistry , vol.38 , pp. 8347-8358
    • Scarsdale, J.N.1    Kazarina, G.2    Radaev, S.3    Schirch, V.4    Wright, H.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.