메뉴 건너뛰기




Volumn 43, Issue 22, 2004, Pages 6865-6876

Serine hydroxymethyltransferase: Role of Glu75 and evidence that serine is cleaved by a retroaldol mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CATALYSIS; ENZYMES; FORMALDEHYDE; HYDROGEN BONDS; MUTAGENESIS;

EID: 2642571803     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049791y     Document Type: Article
Times cited : (60)

References (42)
  • 1
    • 0001042638 scopus 로고
    • Biogenesis and interconversion of substituted tetrahydrofolates
    • (Blakely, R. L., and Benkovic, S. J., Eds.), Wiley, New York
    • MacKenzie, R. E. (1984) Biogenesis and interconversion of substituted tetrahydrofolates, in Folates and Pterins (Blakely, R. L., and Benkovic, S. J., Eds.) Vol. 1, pp 255-306, Wiley, New York.
    • (1984) Folates and Pterins , vol.1 , pp. 255-306
    • MacKenzie, R.E.1
  • 2
    • 0014410177 scopus 로고
    • Serine transhydroxymethylase: Identification as the threonine and allothreonine aldolases
    • Schirch, L., and Gross, T. (1968) Serine transhydroxymethylase: identification as the threonine and allothreonine aldolases, J. Biol. Chem. 243, 5651-5655.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5651-5655
    • Schirch, L.1    Gross, T.2
  • 3
    • 0017761217 scopus 로고
    • Studies of the reactions of substituted D,L-erythro-β-phenylserines with lamb liver serine hydroxymethylase. Effects of substituents upon the dealdolization step
    • Ulevitch, R. J., and Kallen, R. G. (1977) Studies of the reactions of substituted D,L-erythro-β-phenylserines with lamb liver serine hydroxymethylase. Effects of substituents upon the dealdolization step, Biochemistry 16, 5342-5349.
    • (1977) Biochemistry , vol.16 , pp. 5342-5349
    • Ulevitch, R.J.1    Kallen, R.G.2
  • 4
    • 0025160752 scopus 로고
    • Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate
    • Stover, P., and Schirch, V. (1990) Serine hydroxymethyltransferase catalyzes the hydrolysis of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate, J. Biol. Chem. 265, 14227-14233.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14227-14233
    • Stover, P.1    Schirch, V.2
  • 5
    • 0026063520 scopus 로고
    • 5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase
    • Stover, P., and Schirch, V. (1991) 5-Formyltetrahydrofolate polyglutamates are slow tight binding inhibitors of serine hydroxymethyltransferase, J. Biol. Chem. 266, 1543-1550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1543-1550
    • Stover, P.1    Schirch, V.2
  • 6
    • 15644377868 scopus 로고    scopus 로고
    • 5-Formyltetrahydrofolate regulates homocysteine remethylation in human neuroblastoma
    • Girgis, S., Suh, J. R., Jolivet, J., and Stover, P. J. (1997) 5-Formyltetrahydrofolate regulates homocysteine remethylation in human neuroblastoma, J. Biol. Chem. 272, 4729-4734.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4729-4734
    • Girgis, S.1    Suh, J.R.2    Jolivet, J.3    Stover, P.J.4
  • 7
  • 8
    • 0032530853 scopus 로고    scopus 로고
    • The crystal structure of human cytosolic serine hydroxymethyltransferase: A target for cancer chemotherapy
    • Renwick, S. B., Snell, K., and Baumann, U. (1998) The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy, Structure 6, 1105-1116.
    • (1998) Structure , vol.6 , pp. 1105-1116
    • Renwick, S.B.1    Snell, K.2    Baumann, U.3
  • 9
    • 0033614832 scopus 로고    scopus 로고
    • Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: Mechanistic implications
    • Scarsdale, J. N., Radaev, S., Kazanina, G., Schirch, V., and Wright, H. T. (1999) Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 A resolution: mechanistic implications, Biochemistry 38, 8347-8358.
    • (1999) Biochemistry , vol.38 , pp. 8347-8358
    • Scarsdale, J.N.1    Radaev, S.2    Kazanina, G.3    Schirch, V.4    Wright, H.T.5
  • 10
    • 0034619570 scopus 로고    scopus 로고
    • Structure of a murine cytoplasmic serine hydroxymethyltransferase quinonoid ternary complex: Evidence for asymmetric obligate dimers
    • Szebenyi, D. M. E., Liu, X., Kriksunov, I. A., Stover, P. J., and Thiel, D. J. (2000) Structure of a murine cytoplasmic serine hydroxymethyltransferase quinonoid ternary complex: evidence for asymmetric obligate dimers, Biochemistry 39, 13313-13323.
    • (2000) Biochemistry , vol.39 , pp. 13313-13323
    • Szebenyi, D.M.E.1    Liu, X.2    Kriksunov, I.A.3    Stover, P.J.4    Thiel, D.J.5
  • 11
    • 0034635346 scopus 로고    scopus 로고
    • Crystal structure at 2.4 Å resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate
    • Scarsdale, J. N., Radaev, S., Kazanina, G., Schirch, V., and Wright, H. T. (2000) Crystal structure at 2.4 Å resolution of E. coli serine hydroxymethyltransferase in complex with glycine substrate and 5-formyl tetrahydrofolate, J. Mol. Biol. 296, 155-168.
    • (2000) J. Mol. Biol. , vol.296 , pp. 155-168
    • Scarsdale, J.N.1    Radaev, S.2    Kazanina, G.3    Schirch, V.4    Wright, H.T.5
  • 12
    • 0037053283 scopus 로고    scopus 로고
    • Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: Insights into the catalytic mechanism
    • Trivedi, V., Gupta, A., Jala, V. R., Sravanan, P., Rao, G. S. J., Rao, N. A., Savithri, H. S., and Subramanya, H. S. (2002) Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism, J. Biol. Chem. 277, 17161-17169.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17161-17169
    • Trivedi, V.1    Gupta, A.2    Jala, V.R.3    Sravanan, P.4    Rao, G.S.J.5    Rao, N.A.6    Savithri, H.S.7    Subramanya, H.S.8
  • 13
    • 0026645228 scopus 로고
    • Enzymatic mechanism for the hydrolysis of 5,10-methenyltetrahydropteroylglutamate to 5-formyltetrahydropteroylglutamate by serine hydroxymethyltransferase
    • Stover, P., and Schirch, V. (1992) Enzymatic mechanism for the hydrolysis of 5,10-methenyltetrahydropteroylglutamate to 5-formyltetrahydropteroylglutamate by serine hydroxymethyltransferase, Biochemistry 31, 2155-2164.
    • (1992) Biochemistry , vol.31 , pp. 2155-2164
    • Stover, P.1    Schirch, V.2
  • 14
    • 0026642189 scopus 로고
    • Evidence for the accumulation of a stable intermediate in the nonenzymatic hydrolysis of 5,10-methenyltetrahydropteroylglutamate to 5-formyltetrahydropteroylglutamate
    • Stover, P., and Schirch, V. (1992) Evidence for the accumulation of a stable intermediate in the nonenzymatic hydrolysis of 5,10-methenyltetrahydropteroylglutamate to 5-formyltetrahydropteroylglutamate, Biochemistry 31, 2148-2155.
    • (1992) Biochemistry , vol.31 , pp. 2148-2155
    • Stover, P.1    Schirch, V.2
  • 15
    • 0001029771 scopus 로고
    • Providing one-carbon units for biological methylations: Mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase
    • Matthews, R. B., and Drummond, J. T. (1990) Providing one-carbon units for biological methylations: mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase, Chem. Rev. 90, 1275-1290.
    • (1990) Chem. Rev. , vol.90 , pp. 1275-1290
    • Matthews, R.B.1    Drummond, J.T.2
  • 16
    • 0033807968 scopus 로고    scopus 로고
    • The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase
    • Krishna Rao, J. V., Prakash, V., Appaji Rao, N., and Savithri, H. S. (2000) The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase, Eur. J. Biochem. 267, 5967-5976.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5967-5976
    • Krishna Rao, J.V.1    Prakash, V.2    Appaji Rao, N.3    Savithri, H.S.4
  • 17
    • 0030151990 scopus 로고    scopus 로고
    • Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase
    • Iurescia, S., Condò, I., Angelaccio, S., Delle Fratte, S., and Bossa, F. (1996) Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase, Protein Expression Purif. 7, 323-328.
    • (1996) Protein Expression Purif. , vol.7 , pp. 323-328
    • Iurescia, S.1    Condò, I.2    Angelaccio, S.3    Delle Fratte, S.4    Bossa, F.5
  • 18
    • 0025967198 scopus 로고
    • The origin of reaction specificity in serine hydroxymethyltransferase
    • Schirch, V., Shostak, K., Zamora, M., and Gautam-Basak, M. (1991) The origin of reaction specificity in serine hydroxymethyltransferase, J. Biol. Chem. 266, 759-764.
    • (1991) J. Biol. Chem. , vol.266 , pp. 759-764
    • Schirch, V.1    Shostak, K.2    Zamora, M.3    Gautam-Basak, M.4
  • 19
    • 0014043370 scopus 로고
    • Serine transhydroxymethylase, affinity of tetrahydrofolate compounds for the enzyme and enzyme-glycine complex
    • Schirch, L., and Ropp, M. (1967) Serine transhydroxymethylase, affinity of tetrahydrofolate compounds for the enzyme and enzyme-glycine complex, Biochemistry 6, 253-257.
    • (1967) Biochemistry , vol.6 , pp. 253-257
    • Schirch, L.1    Ropp, M.2
  • 20
    • 0026783258 scopus 로고
    • Escherichia coli serine hydroxymethyltransferase: The role of histidine 228 in determining reaction specificity
    • Stover, P., Zamora, M., Shostak, K., Gautam-Basak, M., and Schirch, V. (1992) Escherichia coli serine hydroxymethyltransferase: the role of histidine 228 in determining reaction specificity, J. Biol. Chem. 267, 17679-17687.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17679-17687
    • Stover, P.1    Zamora, M.2    Shostak, K.3    Gautam-Basak, M.4    Schirch, V.5
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0037462648 scopus 로고    scopus 로고
    • Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase
    • Fu, T.-F., Scarsdale, J. N., Kazanina, G., Schirch, V., and Wright, H. T. (2003) Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase, J. Biol. Chem. 278, 2645.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2645
    • Fu, T.-F.1    Scarsdale, J.N.2    Kazanina, G.3    Schirch, V.4    Wright, H.T.5
  • 28
    • 0016661031 scopus 로고
    • Serine transhydroxymethylase: Relaxation and transient kinetic study of the formation and interconversion of the enzyme-glycine complexes
    • Schirch, L. (1975) Serine transhydroxymethylase: relaxation and transient kinetic study of the formation and interconversion of the enzyme-glycine complexes, J. Biol. Chem. 250, 1939-1945.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1939-1945
    • Schirch, L.1
  • 29
    • 0015795321 scopus 로고
    • Serine transhydroxymethylase: A kinetic study of the synthesis of serine in the absence of tetrahydrofolate
    • Chen, M. S., and Schirch, L. (1973) Serine transhydroxymethylase: a kinetic study of the synthesis of serine in the absence of tetrahydrofolate, J. Biol. Chem. 248, 3631-3635.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3631-3635
    • Chen, M.S.1    Schirch, L.2
  • 30
    • 0015730139 scopus 로고
    • Serine transhydroxymethylase: Studies on the role of tetrahydrofolate
    • Chen, M. S., and Schirch, L. (1973) Serine transhydroxymethylase: studies on the role of tetrahydrofolate, J. Biol. Chem. 248, 7979-798.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7979-7798
    • Chen, M.S.1    Schirch, L.2
  • 31
    • 0010522964 scopus 로고
    • Serine transhydroxymethylase: A study of the properties of a homogeneous enzyme preparation and of the nature of its interaction with substrates and pyridoxal 5′-phosphate
    • Schirch, L., and Mason, M. (1963) Serine transhydroxymethylase: a study of the properties of a homogeneous enzyme preparation and of the nature of its interaction with substrates and pyridoxal 5′-phosphate, J. Biol. Chem. 238, 1032-1037.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1032-1037
    • Schirch, L.1    Mason, M.2
  • 32
    • 0026244229 scopus 로고
    • A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 34
    • 0015239671 scopus 로고
    • Serine transhydroxymethylase: Affinity of the active site for substrates, substrate analogues, and anions
    • Schirch, L., and Diller, A. (1971) Serine transhydroxymethylase: affinity of the active site for substrates, substrate analogues, and anions, J. Biol. Chem. 246, 3961-3966.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3961-3966
    • Schirch, L.1    Diller, A.2
  • 35
    • 0013902457 scopus 로고
    • Conformation and reaction specificity in pyridoxal phosphate enzymes
    • Dunathan, H. C. (1966) Conformation and reaction specificity in pyridoxal phosphate enzymes, Proc. Natl. Acad. Sci. U.S.A. 55, 712-716.
    • (1966) Proc. Natl. Acad. Sci. U.S.A. , vol.55 , pp. 712-716
    • Dunathan, H.C.1
  • 37
    • 0025282773 scopus 로고
    • Stereochemistry of reduction of methylenetetrahydrofolate to methyltetrahydrofolate catalyzed by pig liver methylenetetrahydrofolate reductase
    • Vanoni, M. A., Lee, S., Floss, H. G., and Matthews, R. G. (1990) Stereochemistry of reduction of methylenetetrahydrofolate to methyltetrahydrofolate catalyzed by pig liver methylenetetrahydrofolate reductase, J. Am. Chem. Soc. 112, 3987-3992.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3987-3992
    • Vanoni, M.A.1    Lee, S.2    Floss, H.G.3    Matthews, R.G.4
  • 38
    • 0029081865 scopus 로고
    • 4-Chlorothreonine is substrate, mechanistic probe, and mechanism-based inactivator of serine hydroxymethyltransferase
    • Webb, H. K., and Matthews, R. G. (1995) 4-Chlorothreonine is substrate, mechanistic probe, and mechanism-based inactivator of serine hydroxymethyltransferase, J. Biol. Chem. 270, 17204-17209.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17204-17209
    • Webb, H.K.1    Matthews, R.G.2
  • 40
    • 0018267915 scopus 로고
    • Activation of aposerine transhydroxymethylase by pyridoxal-5′ -phosphate monomethyl ester
    • Schirch, L., and Schnackerz, K. D. (1978) Activation of aposerine transhydroxymethylase by pyridoxal-5′-phosphate monomethyl ester, Biochem. Biophys. Res. Commun. 85, 99-106.
    • (1978) Biochem. Biophys. Res. Commun. , vol.85 , pp. 99-106
    • Schirch, L.1    Schnackerz, K.D.2
  • 41
    • 0022967088 scopus 로고    scopus 로고
    • Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis
    • Hopkins, S., and Schirch, V. (1996) Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis, J. Biol. Chem. 261, 3363-3369.
    • (1996) J. Biol. Chem. , vol.261 , pp. 3363-3369
    • Hopkins, S.1    Schirch, V.2
  • 42
    • 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., Rao, N. A., and Savithri, H. S. (1997) The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase, J. Biol. Chem. 272, 24355-24362.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24355-24362
    • Jagath, J.R.1    Sharma, B.2    Rao, N.A.3    Savithri, H.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.