메뉴 건너뛰기




Volumn 283, Issue 1, 1998, Pages 135-146

Catalytic competence of O-acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry

Author keywords

Crystalline protein; Enzyme catalysis; Pyridoxal 5' phosphate; Structure function relationship; X ray crystallography

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; CYSTEINE; SCHIFF BASE; SERINE; SODIUM AZIDE; SULFIDE;

EID: 0032538283     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2038     Document Type: Article
Times cited : (20)

References (44)
  • 1
    • 0030722376 scopus 로고    scopus 로고
    • Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates
    • Benci, S., Vaccari, S., Mozzarelli, A. & Cook, P. F. (1997). Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates. Biochemistry, 36, 15419-15427.
    • (1997) Biochemistry , vol.36 , pp. 15419-15427
    • Benci, S.1    Vaccari, S.2    Mozzarelli, A.3    Cook, P.F.4
  • 3
    • 0017281552 scopus 로고
    • A reaction mechanism from steady-state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2
    • Cook, P. F. & Wedding, R. T. (1976). A reaction mechanism from steady-state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2. J. Biol. Chem. 251, 2023-2029.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2023-2029
    • Cook, P.F.1    Wedding, R.T.2
  • 4
    • 0026511957 scopus 로고
    • 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine
    • 31P NMR spectra of O-acetylserine sulfhydrylase in the absence and presence of O-acetyl-L-serine. Biochemistry, 31, 2298-2303.
    • (1992) Biochemistry , vol.31 , pp. 2298-2303
    • Cook, P.F.1    Hara, S.2    Nalabolu, S.3    Schnackerz, K.D.4
  • 5
    • 0014962790 scopus 로고
    • D-serine dehydratase from Escherichia coli. Analytical studies and subunit structure
    • Dowhan, W., Jr & Snell, E. E. (1970). D-serine dehydratase from Escherichia coli. Analytical studies and subunit structure. J. Biol. Chem. 245, 4618-4628.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4618-4628
    • Dowhan W., Jr.1    Snell, E.E.2
  • 6
    • 0017895426 scopus 로고
    • Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometry
    • Eichele, G., Karabelnik, D., Halobrenner, R., Jansonius, J. N. & Christen, P. (1979). Catalytic activity in crystals of mitochondrial aspartate aminotransferase as detected by microspectrophotometry. J. Biol. Chem. 253, 5239-5242.
    • (1979) J. Biol. Chem. , vol.253 , pp. 5239-5242
    • Eichele, G.1    Karabelnik, D.2    Halobrenner, R.3    Jansonius, J.N.4    Christen, P.5
  • 7
    • 0030056113 scopus 로고    scopus 로고
    • Studies on the synthesis of Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extracts
    • Flint, D. H., Tuminello, J. F. & Miller, T. J. (1996). Studies on the synthesis of Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extracts. J. Biol. Chem. 271, 16053-16067.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16053-16067
    • Flint, D.H.1    Tuminello, J.F.2    Miller, T.J.3
  • 8
    • 0017163151 scopus 로고
    • Stereochemistry of the formation of cysteine by O-acetylserine sulfhydrylase
    • Floss, H. G., Schlerer, E. & Potts, R. (1976). Stereochemistry of the formation of cysteine by O-acetylserine sulfhydrylase. J. Biol. Chem. 251, 5478-5482.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5478-5482
    • Floss, H.G.1    Schlerer, E.2    Potts, R.3
  • 9
    • 0025486959 scopus 로고
    • A rapid purification procedure and a computer assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Hara, S., Payne, M. A., Schnackerz, K. D. & Cook, P. F. (1990). A rapid purification procedure and a computer assisted sulfide ion selective electrode assay for O-acetylserine sulfhydrylase from Salmonella typhimurium. Protein Express. Purif. 1, 70-76.
    • (1990) Protein Express. Purif. , vol.1 , pp. 70-76
    • Hara, S.1    Payne, M.A.2    Schnackerz, K.D.3    Cook, P.F.4
  • 10
    • 0028297538 scopus 로고
    • Crystalline mitochondrial aspartate aminotransferase exists in only two conformations
    • Hohenester, E. & Jansonius, J. N. (1994). Crystalline mitochondrial aspartate aminotransferase exists in only two conformations. J. Mol. Biol. 236, 963-968.
    • (1994) J. Mol. Biol. , vol.236 , pp. 963-968
    • Hohenester, E.1    Jansonius, J.N.2
  • 11
    • 0020756023 scopus 로고
    • Catalytic activity of non-crosslinked microcrystals of aspartate aminotransferase in poly(ethylene) glycol
    • Kirsten, H., Gehring, H. & Christen, P. (1983). Catalytic activity of non-crosslinked microcrystals of aspartate aminotransferase in poly(ethylene) glycol. Biochem. J. 211, 427-434.
    • (1983) Biochem. J. , vol.211 , pp. 427-434
    • Kirsten, H.1    Gehring, H.2    Christen, P.3
  • 12
    • 0028287213 scopus 로고
    • Comparison of the structures and the crystal contacts of trypanosomal triosophosphate isomerase in four different crystal forms
    • Kishan, K. V. R., Zeelen, J. P. H., Noble, M. E. M., Borchert, T. V. & Wierenga, R. K. (1994). Comparison of the structures and the crystal contacts of trypanosomal triosophosphate isomerase in four different crystal forms. Protein Sci. 3, 779-787.
    • (1994) Protein Sci. , vol.3 , pp. 779-787
    • Kishan, K.V.R.1    Zeelen, J.P.H.2    Noble, M.E.M.3    Borchert, T.V.4    Wierenga, R.K.5
  • 13
    • 0019328788 scopus 로고
    • Polarized light absorption spectra of single crystals of aspartate transaminase from chicken heart cytosol
    • Makarov, V. L., Kochkina, V. M. & Torchinsky, Y. M. (1980). Polarized light absorption spectra of single crystals of aspartate transaminase from chicken heart cytosol. FEBS Letters, 114, 79-82.
    • (1980) FEBS Letters , vol.114 , pp. 79-82
    • Makarov, V.L.1    Kochkina, V.M.2    Torchinsky, Y.M.3
  • 14
    • 0017420380 scopus 로고
    • Reactivity and cryoenzymology of enzymes in the crystalline state
    • Makinen, M. W. & Fink, A. L. (1977). Reactivity and cryoenzymology of enzymes in the crystalline state. Annu. Rev. Biophys. Bioeng. 6, 301-343.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 301-343
    • Makinen, M.W.1    Fink, A.L.2
  • 15
    • 0027738034 scopus 로고
    • Crystal structures of true enzymatic reaction intermediates: Aspartate and glutamate ketimines in aspartate aminotransferase
    • Malashkevich, V. N., Toney, M. D. & Jansonius, J. N. (1993). Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Biochemistry, 32, 13451-13462.
    • (1993) Biochemistry , vol.32 , pp. 13451-13462
    • Malashkevich, V.N.1    Toney, M.D.2    Jansonius, J.N.3
  • 16
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 17
    • 0028174296 scopus 로고
    • Product binding to the α-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: Evidence from fluorescence spectroscopy
    • McClure, G. D. & Cook, P. F. (1994). Product binding to the α-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: evidence from fluorescence spectroscopy. Biochemistry, 33, 1674-1683.
    • (1994) Biochemistry , vol.33 , pp. 1674-1683
    • McClure, G.D.1    Cook, P.F.2
  • 19
    • 0023765589 scopus 로고
    • Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase
    • Metzler, C. M., Mitra, J., Metzler, D. E., Makinen, M. W., Hyde, C. C., Rogers, P. & Arnone, A. (1988). Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase. J. Mol. Biol. 203, 197-220.
    • (1988) J. Mol. Biol. , vol.203 , pp. 197-220
    • Metzler, C.M.1    Mitra, J.2    Metzler, D.E.3    Makinen, M.W.4    Hyde, C.C.5    Rogers, P.6    Arnone, A.7
  • 20
    • 0018657645 scopus 로고
    • Tryptophan synthase: Structure, function, and subunit interaction
    • Miles, E. W. (1979). Tryptophan synthase: structure, function, and subunit interaction. Advan. Enzymol. 64, 127-185.
    • (1979) Advan. Enzymol. , vol.64 , pp. 127-185
    • Miles, E.W.1
  • 22
    • 0018497115 scopus 로고
    • Catalytic activity of aspartate aminotransferase in the crystal. Equilibrium and kinetic analysis
    • Mozzarelli, A., Ottonello, S., Rossi, G. L. & Fasella, P. (1979). Catalytic activity of aspartate aminotransferase in the crystal. Equilibrium and kinetic analysis. Eur. J. Biochem. 98, 173-179.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 173-179
    • Mozzarelli, A.1    Ottonello, S.2    Rossi, G.L.3    Fasella, P.4
  • 24
    • 0025801633 scopus 로고
    • Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect
    • Mozzarelli, A., Rivetti, C., Rossi, G. L., Henry, E. R. & Eaton, W. A. (1991). Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature, 351, 416-419.
    • (1991) Nature , vol.351 , pp. 416-419
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Henry, E.R.4    Eaton, W.A.5
  • 25
    • 0031048477 scopus 로고    scopus 로고
    • Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals
    • Mozzarelli, A., Rivetti, C., Rossi, G. L., Eaton, W. A. & Henry, E. R. (1997). Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals. Protein Sci. 6, 484-489.
    • (1997) Protein Sci. , vol.6 , pp. 484-489
    • Mozzarelli, A.1    Rivetti, C.2    Rossi, G.L.3    Eaton, W.A.4    Henry, E.R.5
  • 26
    • 0000907566 scopus 로고
    • Catalytic properties of tryptophanase, a multifunctional pyridoxal phosphate enzyme
    • Newton, W. A. & Snell, E. E. (1964). Catalytic properties of tryptophanase, a multifunctional pyridoxal phosphate enzyme. Proc. Natl Acad. Sci. USA, 51, 382-389.
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 382-389
    • Newton, W.A.1    Snell, E.E.2
  • 27
    • 0030000410 scopus 로고    scopus 로고
    • Crystal structure of T state haemoglobin with oxygen bound at all four haems
    • Paoli, M., Liddington, R., Tame, J., Wilkinson, A. & Dodson, G. (1996). Crystal structure of T state haemoglobin with oxygen bound at all four haems. J. Mol. Biol. 256, 775-792.
    • (1996) J. Mol. Biol. , vol.256 , pp. 775-792
    • Paoli, M.1    Liddington, R.2    Tame, J.3    Wilkinson, A.4    Dodson, G.5
  • 28
  • 30
    • 0027169519 scopus 로고
    • Crystallization and preliminary X-ray data for the A-isoenzyme of O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Rao, G. S. J., Mottonen, J., Goldsmith, E. J. & Cook, P. F. (1993). Crystallization and preliminary X-ray data for the A-isoenzyme of O-acetylserine sulfhydrylase from Salmonella typhimurium. J. Mol. Biol. 231, 1130-1132.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1130-1132
    • Rao, G.S.J.1    Mottonen, J.2    Goldsmith, E.J.3    Cook, P.F.4
  • 31
    • 0029844625 scopus 로고    scopus 로고
    • A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transamination and as a general base catalyst
    • Rege, V. D., Kredich, N. M., Tai, C.-H., Karsten, W. E., Schnackerz, K. D. & Cook, P. F. (1996). A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transamination and as a general base catalyst. Biochemistry, 35, 13485-13493.
    • (1996) Biochemistry , vol.35 , pp. 13485-13493
    • Rege, V.D.1    Kredich, N.M.2    Tai, C.-H.3    Karsten, W.E.4    Schnackerz, K.D.5    Cook, P.F.6
  • 32
    • 0030800147 scopus 로고    scopus 로고
    • 2 complex with ligands bound to the active sites of the a- And β-subunits reveal ligand-induced conformational changes
    • 2 complex with ligands bound to the active sites of the a- and β-subunits reveal ligand-induced conformational changes. Biochemistry, 36, 7664-7680.
    • (1997) Biochemistry , vol.36 , pp. 7664-7680
    • Rhee, S.1    Parris, K.D.2    Hyde, C.C.3    Ahmed, S.A.4    Miles, E.W.5    Davies, D.R.6
  • 33
    • 0344087421 scopus 로고
    • Structure of proteins
    • Richards, F. M. (1963). Structure of proteins. Annu. Rev. Biochem. 32, 269-300.
    • (1963) Annu. Rev. Biochem. , vol.32 , pp. 269-300
    • Richards, F.M.1
  • 35
    • 0014944889 scopus 로고
    • Are the structure and function of an enzyme the same in aqueous solution and in the wet crystal?
    • Rossi, G. L. & Berhnard, S. A. (1970). Are the structure and function of an enzyme the same in aqueous solution and in the wet crystal? J. Mol. Biol. 49, 85-91.
    • (1970) J. Mol. Biol. , vol.49 , pp. 85-91
    • Rossi, G.L.1    Berhnard, S.A.2
  • 36
    • 0000206688 scopus 로고
    • Time course of chemical and structural events in protein crystals measured by microspectrophotometry
    • Rossi, G. L., Mozzarelli, A., Peracchi, A. & Rivetti, C. (1992). Time course of chemical and structural events in protein crystals measured by microspectrophotometry. Phil. Trans. Roy. Soc. ser. A, 340, 191-207.
    • (1992) Phil. Trans. Roy. Soc. Ser. A , vol.340 , pp. 191-207
    • Rossi, G.L.1    Mozzarelli, A.2    Peracchi, A.3    Rivetti, C.4
  • 37
    • 0019887948 scopus 로고
    • Microspectrophotometric measurements on single crystals of mitochondrial serine hydroxymethyltransferase
    • Schirch, L. V., Mozzarelli, A., Ottonello, S. & Rossi, G. L. (1981). Microspectrophotometric measurements on single crystals of mitochondrial serine hydroxymethyltransferase. J. Biol. Chem. 256, 3776-3780.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3776-3780
    • Schirch, L.V.1    Mozzarelli, A.2    Ottonello, S.3    Rossi, G.L.4
  • 38
    • 0029089919 scopus 로고
    • Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction
    • Schnackerz, K. D., Tai, C.-H., Simmons, J. W., Jacobson, T. M., Rao, J. G. S. & Cook, P. F. (1995). Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction. Biochemistry, 34, 12152-12160.
    • (1995) Biochemistry , vol.34 , pp. 12152-12160
    • Schnackerz, K.D.1    Tai, C.-H.2    Simmons, J.W.3    Jacobson, T.M.4    Rao, J.G.S.5    Cook, P.F.6
  • 40
    • 0030059159 scopus 로고    scopus 로고
    • Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway
    • Strambini, G., Cioni, P. & Cook, P. F. (1996). Tryptophan luminescence as a probe of enzyme conformation along the O-acetylserine sulfhydrylase reaction pathway. Biochemistry, 35, 8392-8400.
    • (1996) Biochemistry , vol.35 , pp. 8392-8400
    • Strambini, G.1    Cioni, P.2    Cook, P.F.3
  • 41
    • 0027183564 scopus 로고
    • Kinetic mechanism of the a and B isoenzymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Tai, C.-H., Nalabolu, S. R., Jacobson, T. M., Hinter, D. E. & Cook, P. F. (1993). Kinetic mechanism of the A and B isoenzymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants. Biochemistry, 32, 6433-6442.
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.-H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Hinter, D.E.4    Cook, P.F.5
  • 42
    • 0013627149 scopus 로고    scopus 로고
    • Time-resolved fluorescence of pyridoxal 5'-phosphate-containing enzymes: Tryptophan synthase and O-acetylserine sulfhydrylase
    • Vaccari, S., Benci, S., Peracchi, A. & Mozzarelli, A. (1997). Time-resolved fluorescence of pyridoxal 5'-phosphate-containing enzymes: tryptophan synthase and O-acetylserine sulfhydrylase. J. Fluor. 7, 135S-137S.
    • (1997) J. Fluor. , vol.7
    • Vaccari, S.1    Benci, S.2    Peracchi, A.3    Mozzarelli, A.4
  • 44
    • 0029865896 scopus 로고    scopus 로고
    • Formation of the α-aminoacrylate intermediate limits the overall reaction catalyzed by O-acetyl-serine sulfhydrylase
    • Woehl, E. U., Tai, C.-H., Dunn, M. F. & Cook, P. F. (1996). Formation of the α-aminoacrylate intermediate limits the overall reaction catalyzed by O-acetyl-serine sulfhydrylase. Biochemistry, 35, 4776-4783.
    • (1996) Biochemistry , vol.35 , pp. 4776-4783
    • Woehl, E.U.1    Tai, C.-H.2    Dunn, M.F.3    Cook, P.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.