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Volumn 7, Issue 9, 1998, Pages 1976-1982

The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis

Author keywords

Aspartate aminotransferase; Catalysis; Evolution; Homology modeling; Profile analysis; Pyridoxal phosphate; Serine hydroxymethyltransferase; Site directed mutagenesis

Indexed keywords

ASPARTATE AMINOTRANSFERASE; CARBOXYLYASE; METHYLTRANSFERASE; MUTANT PROTEIN; SERINE HYDROMETHYLTRANSFERASE; TYROSINE PHENOL LYASE; UNCLASSIFIED DRUG;

EID: 0031709347     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070913     Document Type: Article
Times cited : (8)

References (45)
  • 1
    • 0028044574 scopus 로고
    • Evolutionary relationship among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific α, β and γ families
    • Alexander F, Sandmeier E, Mehta PK, Christen P. 1994. Evolutionary relationship among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific α, β and γ families. Eur J Biochem 219:953-960.
    • (1994) Eur J Biochem , vol.219 , pp. 953-960
    • Alexander, F.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4
  • 4
    • 0025796712 scopus 로고
    • The SWISS-PROT protein sequence data bank
    • Bairoch A, Boeckmann B. 1991. The SWISS-PROT protein sequence data bank. Nucleic Acids Res 19:2247-2249.
    • (1991) Nucleic Acids Res , vol.19 , pp. 2247-2249
    • Bairoch, A.1    Boeckmann, B.2
  • 6
    • 0017092198 scopus 로고
    • Serine transhydroxymethylase from rabbit liver. Sequence of a nonapeptide at the pyridoxal-5‴-phosphate-binding site
    • Bossa F, Barra D, Martini F, Schirch LV, Fasella P. 1976. Serine transhydroxymethylase from rabbit liver. Sequence of a nonapeptide at the pyridoxal-5‴-phosphate-binding site. Eur J Biochem 70:397-401.
    • (1976) Eur J Biochem , vol.70 , pp. 397-401
    • Bossa, F.1    Barra, D.2    Martini, F.3    Schirch, L.V.4    Fasella, P.5
  • 7
    • 0028040757 scopus 로고
    • The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase
    • Delle Fratte S, Iurescia S, Angelaccio S, Bossa F, Schirch V. 1994. The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase. Eur J Biochem 225: 395-401.
    • (1994) Eur J Biochem , vol.225 , pp. 395-401
    • Delle Fratte, S.1    Iurescia, S.2    Angelaccio, S.3    Bossa, F.4    Schirch, V.5
  • 8
    • 0013902457 scopus 로고
    • Conformation and reaction specificity in pyridoxal phosphate enzymes
    • Dunathan HC. 1966. Conformation and reaction specificity in pyridoxal phosphate enzymes. Proc Natl Acad Sci USA 55:712-716.
    • (1966) Proc Natl Acad Sci USA , vol.55 , pp. 712-716
    • Dunathan, H.C.1
  • 10
    • 0019888748 scopus 로고
    • Comparative model-building of the mammalian serine proteases
    • Greer J. 1981. Comparative model-building of the mammalian serine proteases. J Mol Biol 153:1027-1042.
    • (1981) J Mol Biol , vol.153 , pp. 1027-1042
    • Greer, J.1
  • 12
    • 0029080677 scopus 로고
    • Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: Involvement of Tyr70 in stabilization of the catalytic intermediates
    • Hayashi H, Kagamiyama H. 1995. Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: Involvement of Tyr70 in stabilization of the catalytic intermediates. Biochemistry 34:9413-9423.
    • (1995) Biochemistry , vol.34 , pp. 9413-9423
    • Hayashi, H.1    Kagamiyama, H.2
  • 14
    • 0022967088 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, Schirch V. 1986. 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.
    • (1986) J Biol Chem , vol.261 , pp. 3363-3369
    • Hopkins, S.1    Schirch, V.2
  • 15
    • 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, Bossa F. 1996. Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase. Protein Expr Purif 7:323-328.
    • (1996) Protein Expr Purif , vol.7 , pp. 323-328
    • Iurescia, S.1    Condò, I.2    Angelaccio, S.3    Delle Fratte, S.4    Bossa, F.5
  • 16
    • 0030800643 scopus 로고    scopus 로고
    • The role of His-143, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase
    • Jagath JR, Sharma B, Appaji Rao N, Savithri HS. 1997. The role of His-143, -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    Appaji Rao, N.3    Savithri, H.S.4
  • 17
    • 0025279371 scopus 로고
    • The role of a critical sulfhydryl group in the mechanism of serine hydroxymethyltransferase
    • Joshi-Tope G, Schirch V. 1990. The role of a critical sulfhydryl group in the mechanism of serine hydroxymethyltransferase. Annals NY Acad Sci 585:339-345.
    • (1990) Annals NY Acad Sci , vol.585 , pp. 339-345
    • Joshi-Tope, G.1    Schirch, V.2
  • 19
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis J. 1991. Molscript: 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, J.1
  • 20
  • 21
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Lüthy R, Bowie JU, Eisenberg D. 1992. Assessment of protein models with three-dimensional profiles. Nature 356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Lüthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 22
    • 0026093211 scopus 로고
    • A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase- And tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protins of glycine
    • Malthouse JPG, Milne JJ, Gariani LS. 1991. A comparative study of the kinetics and stereochemistry of the serine hydroxymethyltransferase-and tryptophan synthase-catalysed exchange of the pro-2R and pro-2S protins of glycine. Biochem J 274:807-812.
    • (1991) Biochem J , vol.274 , pp. 807-812
    • Malthouse, J.P.G.1    Milne, J.J.2    Gariani, L.S.3
  • 24
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 25
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • McPhalen CA, Vincent MG, Jansonius JN. 1992. X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J Mol Biol 225:495-517.
    • (1992) J Mol Biol , vol.225 , pp. 495-517
    • McPhalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 26
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta PK, Hale TI, Christen P. 1993. Aminotransferases: Demonstration of homology and division into evolutionary subgroups. Eur J Biochem 274:549-561.
    • (1993) Eur J Biochem , vol.274 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 27
    • 0029131487 scopus 로고
    • Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution
    • Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML. 1995a. Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution. J Mol Biol 252:643-655.
    • (1995) J Mol Biol , vol.252 , pp. 643-655
    • Momany, C.1    Ernst, S.2    Ghosh, R.3    Chang, N.L.4    Hackert, M.L.5
  • 28
    • 0028921425 scopus 로고
    • Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacilus 30a ornithine decarboxylase
    • Momany C, Ghosh R, Hackert ML. 1995b. Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: An analysis based on the crystal structure of the Lactobacilus 30a ornithine decarboxylase. Protein Sci 4:849-854
    • (1995) Protein Sci , vol.4 , pp. 849-854
    • Momany, C.1    Ghosh, R.2    Hackert, M.L.3
  • 29
    • 0028167665 scopus 로고
    • X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferase from Escherichia coli in open and closed form
    • Okamoto A, Higuchi T, Hirotsu K, Kuramitsu S, Kagamiyama H. 1994. X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferase from Escherichia coli in open and closed form. J Biochem 116:95-107.
    • (1994) J Biochem , vol.116 , pp. 95-107
    • Okamoto, A.1    Higuchi, T.2    Hirotsu, K.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 30
    • 0027366667 scopus 로고
    • Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzymes
    • Pascarella S, Schirch V, Bossa F. 1993. Similarity between serine hydroxymethyltransferase and other pyridoxal phosphate-dependent enzymes. FEBS Lett 331:145-149.
    • (1993) FEBS Lett , vol.331 , pp. 145-149
    • Pascarella, S.1    Schirch, V.2    Bossa, F.3
  • 31
    • 0025501235 scopus 로고
    • NRL_3D: A sequence-structure database derived from the protein data bank (PDB) and searchable within the PIR environment
    • Pattabiraman N, Namboodiri K, Lowrey A, Gaber BP. 1990. NRL_3D: A sequence-structure database derived from the protein data bank (PDB) and searchable within the PIR environment. Protein Seq Data Anal 3:387-405.
    • (1990) Protein Seq Data Anal , vol.3 , pp. 387-405
    • Pattabiraman, N.1    Namboodiri, K.2    Lowrey, A.3    Gaber, B.P.4
  • 32
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-77.
    • (1994) Proteins , vol.19 , pp. 55-77
    • Rost, B.1    Sander, C.2
  • 33
    • 0031577260 scopus 로고    scopus 로고
    • Fold recognition by prediction-based threading
    • Rost B, Schneider R, Sander C. 1997. Fold recognition by prediction-based threading. J Mol Biol 270:1-10.
    • (1997) J Mol Biol , vol.270 , pp. 1-10
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 35
    • 0027136282 scopus 로고
    • Comparative protein modelling by statisfaction of spatial restraints
    • Šali A, Blundell TL. 1993. Comparative protein modelling by statisfaction of spatial restraints. J Mol Biol 234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 37
    • 0020005825 scopus 로고
    • Serine hydroxymethyltransferase
    • Schirch V. 1982. Serine hydroxymethyltransferase. Adv Enzymol 53:83-111.
    • (1982) Adv Enzymol , vol.53 , pp. 83-111
    • Schirch, V.1
  • 38
    • 0028172555 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase
    • Shen BW, Ramesh V, Müller R, Hohenester E, Hennig M, Jansonius JN. 1994. Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase. J Mol Biol 243:128-130.
    • (1994) J Mol Biol , vol.243 , pp. 128-130
    • Shen, B.W.1    Ramesh, V.2    Müller, R.3    Hohenester, E.4    Hennig, M.5    Jansonius, J.N.6
  • 39
    • 0024291314 scopus 로고
    • Serine hydroxymethyltransferase: Mechanism of the racemization and transamination of D- and L-alanine
    • Shostak K, Schirch V. 1988. Serine hydroxymethyltransferase: Mechanism of the racemization and transamination of D-and L-alanine. Biochemistry 27:8007-8014.
    • (1988) Biochemistry , vol.27 , pp. 8007-8014
    • Shostak, K.1    Schirch, V.2
  • 40
    • 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, 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
  • 41
    • 0028885266 scopus 로고
    • Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase
    • Toney MD, Hohenester E, Keller JW, Jansonius JN. 1995. Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase. J Mol Biol 245:151-179.
    • (1995) J Mol Biol , vol.245 , pp. 151-179
    • Toney, M.D.1    Hohenester, E.2    Keller, J.W.3    Jansonius, J.N.4
  • 42
    • 0029046744 scopus 로고
    • An assessment of amino acid exchange matrices in aligning protein sequences: The twilight zone revisited
    • Vogt G, Etzold T, Argos P. 1995. An assessment of amino acid exchange matrices in aligning protein sequences: The twilight zone revisited. J Mol Biol 249:816-831.
    • (1995) J Mol Biol , vol.249 , pp. 816-831
    • Vogt, G.1    Etzold, T.2    Argos, P.3
  • 43
    • 20244378184 scopus 로고
    • Crystal structure analysis of ω-aminoacid: Pyruvate aminotransferase with newly developed Weissenberg camera and an imaging plate using synchrotron radiation
    • Watanabe N, Sakabe N, Sakabe K, Higashi T, Sasaki K, Aibara S, Morita Y, Yonoha K, Toyama S, Fukutani H. 1989. Crystal structure analysis of ω-aminoacid: Pyruvate aminotransferase with newly developed Weissenberg camera and an imaging plate using synchrotron radiation. J Biochem 105:1-3
    • (1989) J Biochem , vol.105 , pp. 1-3
    • Watanabe, N.1    Sakabe, N.2    Sakabe, K.3    Higashi, T.4    Sasaki, K.5    Aibara, S.6    Morita, Y.7    Yonoha, K.8    Toyama, S.9    Fukutani, H.10
  • 44
    • 0025922823 scopus 로고
    • The role of His-143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase
    • Yano T, Kuramitsu S, Tanase S, Morino Y, Hiromi K, Kagamiyama H. 1991. The role of His-143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. J Biol Chem 266:6079-6085.
    • (1991) J Biol Chem , vol.266 , pp. 6079-6085
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Hiromi, K.5    Kagamiyama, H.6
  • 45
    • 0026664513 scopus 로고
    • Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal-5′-phosphate
    • Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H. 1992. Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: The amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal-5′-phosphate. Biochemistry 31:5878-5887.
    • (1992) Biochemistry , vol.31 , pp. 5878-5887
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Kagamiyama, H.5


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