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Volumn 24, Issue 1, 1999, Pages 69-77

Guanidine hydrochloride-induced reversible unfolding of sheep liver serine hydroxymethyltransferase

Author keywords

GdnHCl denaturation; Oligomeric proteins; PLP dependent enzymes; Reversible unfolding; Serine hydroxymethyltransferase

Indexed keywords

GLYCINE HYDROXYMETHYLTRANSFERASE; GUANIDINE;

EID: 0032931341     PISSN: 02505991     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02941109     Document Type: Article
Times cited : (1)

References (24)
  • 1
    • 0026775163 scopus 로고
    • A novel intermediate in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase
    • Acharya J K and Rao N A 1992 A novel intermediate in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase; J. Biol. Chem. 267 19066-19071
    • (1992) J. Biol. Chem. , vol.267 , pp. 19066-19071
    • Acharya, J.K.1    Rao, N.A.2
  • 3
    • 0028033730 scopus 로고
    • Interactions of L-serine at the active site of serine hydroxymethyltransferases: Induction of thermal stability
    • Bhaskar B, Prakash V, Savithri H S and Rao N A 1994 Interactions of L-serine at the active site of serine hydroxymethyltransferases: induction of thermal stability; Biochim. Biophys. Acta 1209 40-50
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 40-50
    • Bhaskar, B.1    Prakash, V.2    Savithri, H.S.3    Rao, N.A.4
  • 4
    • 0022343373 scopus 로고
    • Kinetics and importance of the dimerization step in the folding pathway of beta 2 subunit of Escherichia coli tryptophan synthase
    • Blond S and Goldberg M E 1985 Kinetics and importance of the dimerization step in the folding pathway of beta 2 subunit of Escherichia coli tryptophan synthase; J. Mol. Biol. 182 597-606
    • (1985) J. Mol. Biol. , vol.182 , pp. 597-606
    • Blond, S.1    Goldberg, M.E.2
  • 5
    • 0029943650 scopus 로고    scopus 로고
    • Interaction of sheep liver apo-serine hydroxymethyltransferase with pyridoxal-5′-phosphate: A physicochemical, kinetic and thermodynamic study
    • Brahatheeswaran B, Prakash V, Savithri H S and Rao N A 1996 Interaction of sheep liver apo-serine hydroxymethyltransferase with pyridoxal-5′-phosphate: A physicochemical, kinetic and thermodynamic study; Arch. Biochem. Biophys. 330 363-372
    • (1996) Arch. Biochem. Biophys. , vol.330 , pp. 363-372
    • Brahatheeswaran, B.1    Prakash, V.2    Savithri, H.S.3    Rao, N.A.4
  • 6
    • 0030019662 scopus 로고    scopus 로고
    • Structural studies on folding intermediates of serine hydroxymethyltransferase using single tryptophan mutants
    • Cai K and Schirch V 1996a Structural studies on folding intermediates of serine hydroxymethyltransferase using single tryptophan mutants; J. Biol. Chem. 271 2987-2994
    • (1996) J. Biol. Chem. , vol.271 , pp. 2987-2994
    • Cai, K.1    Schirch, V.2
  • 7
    • 0029910143 scopus 로고    scopus 로고
    • Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer
    • Cai K and Schirch V 1996b Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer; J. Biol. Chem. 271 27311-27320
    • (1996) J. Biol. Chem. , vol.271 , pp. 27311-27320
    • Cai, K.1    Schirch, V.2
  • 8
    • 0029095080 scopus 로고
    • The affinity of pyridoxal-5′-phosphate for folding intermediates of E. coli serine hydroxymethyltransferase
    • Cai K, Schirch D and Schirch V 1995 The affinity of pyridoxal-5′-phosphate for folding intermediates of E. coli serine hydroxymethyltransferase; J. Biol. Chem. 270 19294-19299
    • (1995) J. Biol. Chem. , vol.270 , pp. 19294-19299
    • Cai, K.1    Schirch, D.2    Schirch, V.3
  • 9
    • 0016292941 scopus 로고
    • Urea and GdnHCl denaturation of ribonuclease, lysozyme, α-chymotrypsin and β-lactoglobulin
    • Greene R F and Pace C N 1974 Urea and GdnHCl denaturation of ribonuclease, lysozyme, α-chymotrypsin and β-lactoglobulin; J. Biol. Chem. 249 5388-5393
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Greene, R.F.1    Pace, C.N.2
  • 11
    • 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, Rao N A and Savithri H S 1997a Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase; Eur. J. Biochem. 247 372-379
    • (1997) Eur. J. Biochem. , vol.247 , pp. 372-379
    • Jagath, J.R.1    Sharma, B.2    Bhaskar, B.3    Datta, A.4    Rao, N.A.5    Savithri, H.S.6
  • 12
    • 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 1997b 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
  • 13
    • 0030660382 scopus 로고    scopus 로고
    • Role of Arg-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group
    • Jagath J R, Rao N A and Savithri H S 1997c Role of Arg-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group; Biochem. J. 327 877-882
    • (1997) Biochem. J. , vol.327 , pp. 877-882
    • Jagath, J.R.1    Rao, N.A.2    Savithri, H.S.3
  • 14
    • 0014940780 scopus 로고
    • The tryptophan microenvironments in apomyoglobin
    • Kirby E P and Steiner R F 1970 The tryptophan microenvironments in apomyoglobin; J. Biol. Chem. 245 6300-6306
    • (1970) J. Biol. Chem. , vol.245 , pp. 6300-6306
    • Kirby, E.P.1    Steiner, R.F.2
  • 15
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
    • Kuwajima K 1989 The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure; Proteins Struct. Func. Genet. 6 87-103
    • (1989) Proteins Struct. Func. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 17
    • 51249180801 scopus 로고
    • Purification, physicochemical regulatory properties of serine hydroxymethyltransferase from sheep liver
    • Manohar R, Ramesh K S and Rao N A 1982 Purification, physicochemical regulatory properties of serine hydroxymethyltransferase from sheep liver; J. Biosci. 4 31-50
    • (1982) J. Biosci. , vol.4 , pp. 31-50
    • Manohar, R.1    Ramesh, K.S.2    Rao, N.A.3
  • 18
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews C R 1993 Pathways of protein folding; Annu. Rev. Biochem. 62 653-683
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 19
    • 0028915773 scopus 로고
    • Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue leads to accumulation of at least one equilibrium folding intermediate
    • Nath U and Udgaonkar J B 1995 Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue leads to accumulation of at least one equilibrium folding intermediate; Biochemistry 34 1702-1713
    • (1995) Biochemistry , vol.34 , pp. 1702-1713
    • Nath, U.1    Udgaonkar, J.B.2
  • 21
    • 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
  • 23
    • 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 and Rao N A 1997 The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase; Acta Biochim. Pol. 44 679-688
    • (1997) Acta Biochim. Pol. , vol.44 , pp. 679-688
    • Talwar, R.1    Jagath, J.R.2    Datta, A.3    Prakash, V.4    Savithri, H.S.5    Rao, N.A.6
  • 24
    • 0032560031 scopus 로고    scopus 로고
    • Reversible unfolding of sheep liver tetrameric serine hydroxymethyltransferase
    • Venkatesha B, Udgaonkar J B, Rao N A and Savithri H S 1998 Reversible unfolding of sheep liver tetrameric serine hydroxymethyltransferase; Biochim. Biophys. Acta 1384 141-152
    • (1998) Biochim. Biophys. Acta , vol.1384 , pp. 141-152
    • Venkatesha, B.1    Udgaonkar, J.B.2    Rao, N.A.3    Savithri, H.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.