메뉴 건너뛰기




Volumn 422, Issue 1, 2012, Pages 33-44

Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon aeropyrum pernix K1

Author keywords

arginine 297; O phosphoserine sulfhydrylase; phosphate group; the external Schiff base of mutant enzyme with its substrate; thermostable enzyme

Indexed keywords

CARBOXYLIC ACID; LYSINE; PHOSPHOSERINE; PYRIDOXAL 5 PHOSPHATE; SCHIFF BASE; SERINE;

EID: 84864621172     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.05.009     Document Type: Article
Times cited : (14)

References (46)
  • 1
    • 0026738588 scopus 로고
    • The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli
    • Kredich N.M. The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli Mol. Microbiol. 6 1992 2747 2753
    • (1992) Mol. Microbiol. , vol.6 , pp. 2747-2753
    • Kredich, N.M.1
  • 2
    • 0030904866 scopus 로고    scopus 로고
    • Molecular physiology of plant sulfur metabolism
    • Hell R. Molecular physiology of plant sulfur metabolism Planta 202 1997 138 148
    • (1997) Planta , vol.202 , pp. 138-148
    • Hell, R.1
  • 3
    • 33644685874 scopus 로고    scopus 로고
    • Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana
    • Bonner E.R., Cahoon R.E., Knapke S.M., and Jez J.M. Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana J. Biol. Chem. 280 2005 38803 38813
    • (2005) J. Biol. Chem. , vol.280 , pp. 38803-38813
    • Bonner, E.R.1    Cahoon, R.E.2    Knapke, S.M.3    Jez, J.M.4
  • 4
    • 33947545688 scopus 로고    scopus 로고
    • Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
    • Francois J.A., Kumaran S., and Jez J.M. Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex Plant Cell 18 2006 3647 3655
    • (2006) Plant Cell , vol.18 , pp. 3647-3655
    • Francois, J.A.1    Kumaran, S.2    Jez, J.M.3
  • 5
    • 0034251888 scopus 로고    scopus 로고
    • Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics
    • Mino K., Yamanoue T., Sakiyama T., Eisaki N., Matsuyama A., and Nakanishi K. Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics Biosci. Biotechnol. Biochem. 64 2000 1628 1640
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1628-1640
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 6
    • 20544435016 scopus 로고    scopus 로고
    • Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli
    • Claus M.T., Zocher G.E., Maier T.H., and Schulz G.E. Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli Biochemistry 44 2005 8620 8626
    • (2005) Biochemistry , vol.44 , pp. 8620-8626
    • Claus, M.T.1    Zocher, G.E.2    Maier, T.H.3    Schulz, G.E.4
  • 7
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • Rabeh W.M., and Cook P.F. Structure and mechanism of O-acetylserine sulfhydrylase J. Biol. Chem. 279 2004 26803 26806
    • (2004) J. Biol. Chem. , vol.279 , pp. 26803-26806
    • Rabeh, W.M.1    Cook, P.F.2
  • 9
    • 0033609810 scopus 로고    scopus 로고
    • Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Burkhard P., Tai C.H., Ristroph C.M., Cook P.F., and Jansonius J.N. Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium J. Mol. Biol. 291 1999 941 953
    • (1999) J. Mol. Biol. , vol.291 , pp. 941-953
    • Burkhard, P.1    Tai, C.H.2    Ristroph, C.M.3    Cook, P.F.4    Jansonius, J.N.5
  • 10
    • 34447554594 scopus 로고    scopus 로고
    • Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: Comparison of A and B isozymes
    • Chattopadhyay A., Meier M., Ivaninskii S., Burkhard P., Speroni F., and Campanini B. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes Biochemistry 46 2007 8315 8330
    • (2007) Biochemistry , vol.46 , pp. 8315-8330
    • Chattopadhyay, A.1    Meier, M.2    Ivaninskii, S.3    Burkhard, P.4    Speroni, F.5    Campanini, B.6
  • 11
    • 58149488752 scopus 로고    scopus 로고
    • The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity
    • Agren D., Schnell R., and Schneider G. The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity FEBS Lett. 583 2009 330 336
    • (2009) FEBS Lett. , vol.583 , pp. 330-336
    • Agren, D.1    Schnell, R.2    Schneider, G.3
  • 12
    • 55249100956 scopus 로고    scopus 로고
    • O-phospho-l-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis
    • O'Leary S.E., Jurgenson C.T., Ealick S.E., and Begley T.P. O-phospho-l-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis Biochemistry 47 2008 11606 11615
    • (2008) Biochemistry , vol.47 , pp. 11606-11615
    • O'Leary, S.E.1    Jurgenson, C.T.2    Ealick, S.E.3    Begley, T.P.4
  • 13
    • 52949126017 scopus 로고    scopus 로고
    • Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis
    • Jurgenson C.T., Burns K.E., Begley T.P., and Ealick S.E. Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis Biochemistry 47 2008 10354 10364
    • (2008) Biochemistry , vol.47 , pp. 10354-10364
    • Jurgenson, C.T.1    Burns, K.E.2    Begley, T.P.3    Ealick, S.E.4
  • 14
    • 57649136751 scopus 로고    scopus 로고
    • Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: Evidence for an alternative cysteine biosynthesis pathway in Mycobacteria
    • Agren D., Schnell R., Oehlmann W., Singh M., and Schneider G. Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in Mycobacteria J. Biol. Chem. 283 2008 31567 31574
    • (2008) J. Biol. Chem. , vol.283 , pp. 31567-31574
    • Agren, D.1    Schnell, R.2    Oehlmann, W.3    Singh, M.4    Schneider, G.5
  • 15
    • 34548188995 scopus 로고    scopus 로고
    • Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex
    • Schnell R., Oehlmann W., Singh M., and Schneider G. Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex J. Biol. Chem. 282 2007 23473 23481
    • (2007) J. Biol. Chem. , vol.282 , pp. 23473-23481
    • Schnell, R.1    Oehlmann, W.2    Singh, M.3    Schneider, G.4
  • 16
    • 33748755115 scopus 로고    scopus 로고
    • Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine
    • Westrop G.D., Goodall G., Mottram J.C., and Coombs G.H. Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine J. Biol. Chem. 281 2006 25062 25075
    • (2006) J. Biol. Chem. , vol.281 , pp. 25062-25075
    • Westrop, G.D.1    Goodall, G.2    Mottram, J.C.3    Coombs, G.H.4
  • 17
    • 0032583190 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the genes encoding two isoforms of cysteine synthase in the enteric protozoan parasite Entamoeba histolytica
    • Nozaki T., Asai T., Kobayashi S., Ikegami F., Noji M., Saito K., and Takeuchi T. Molecular cloning and characterization of the genes encoding two isoforms of cysteine synthase in the enteric protozoan parasite Entamoeba histolytica Mol. Biochem. Parasitol. 97 1998 33 44
    • (1998) Mol. Biochem. Parasitol. , vol.97 , pp. 33-44
    • Nozaki, T.1    Asai, T.2    Kobayashi, S.3    Ikegami, F.4    Noji, M.5    Saito, K.6    Takeuchi, T.7
  • 18
    • 51349147518 scopus 로고    scopus 로고
    • Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: Structural evidence for cysteine binding and lack of interactions with serine acetyl transferase
    • Chinthalapudi K., Kumar M., Kumar S., Jain S., Alam N., and Gourinath S. Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase Proteins 72 2008 1222 1232
    • (2008) Proteins , vol.72 , pp. 1222-1232
    • Chinthalapudi, K.1    Kumar, M.2    Kumar, S.3    Jain, S.4    Alam, N.5    Gourinath, S.6
  • 19
    • 0009056610 scopus 로고
    • Heterocyclic β-substituted alanines
    • P.J. Lea, Academic Press London, UK
    • Ikegami F., and Murakoshi I. Heterocyclic β-substituted alanines P.J. Lea, Methods in Plant Biochemistry vol. 9 1993 Academic Press London, UK 133 151
    • (1993) Methods in Plant Biochemistry , vol.9 VOL. , pp. 133-151
    • Ikegami, F.1    Murakoshi, I.2
  • 20
    • 0030056113 scopus 로고    scopus 로고
    • Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis
    • Flint D.H., Tuminello J.F., and Miller T.J. Studies on the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase in Escherichia coli crude extract. Isolation of O-acetylserine sulfhydrylases A and B and beta-cystathionase based on their ability to mobilize sulfur from cysteine and to participate in Fe-S cluster synthesis J. Biol. Chem. 271 1996 16053 16067
    • (1996) J. Biol. Chem. , vol.271 , pp. 16053-16067
    • Flint, D.H.1    Tuminello, J.F.2    Miller, T.J.3
  • 21
    • 0031031385 scopus 로고    scopus 로고
    • Production of plant non-protein amino acids by recombinant enzymes of sequential biosynthetic reactions in bacteria
    • Saito K., Kimura N., Ikegami F., and Noji M. Production of plant non-protein amino acids by recombinant enzymes of sequential biosynthetic reactions in bacteria Biol. Pharm. Bull. 20 1997 47 53
    • (1997) Biol. Pharm. Bull. , vol.20 , pp. 47-53
    • Saito, K.1    Kimura, N.2    Ikegami, F.3    Noji, M.4
  • 22
    • 0037385630 scopus 로고    scopus 로고
    • Semisynthetic production of unnatural l-alpha-amino acids by metabolic engineering of the cysteine-biosynthetic pathway
    • Maier T.H. Semisynthetic production of unnatural l-alpha-amino acids by metabolic engineering of the cysteine-biosynthetic pathway Nat. Biotechnol. 21 2003 422 427
    • (2003) Nat. Biotechnol. , vol.21 , pp. 422-427
    • Maier, T.H.1
  • 23
    • 2942594379 scopus 로고    scopus 로고
    • Production of nonproteinaceous amino acids using recombinant Escherichia coli cells expressing cysteine synthase and related enzymes with or without the secretion of O-acetyl-l-serine
    • Zhao C., Ohno K., Sogoh K., Imamura K., Sakiyama T., and Nakanishi K. Production of nonproteinaceous amino acids using recombinant Escherichia coli cells expressing cysteine synthase and related enzymes with or without the secretion of O-acetyl-l-serine J. Biosci. Bioeng. 97 2004 322 328
    • (2004) J. Biosci. Bioeng. , vol.97 , pp. 322-328
    • Zhao, C.1    Ohno, K.2    Sogoh, K.3    Imamura, K.4    Sakiyama, T.5    Nakanishi, K.6
  • 24
    • 16844378688 scopus 로고    scopus 로고
    • Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction
    • Rabeh W.M., Alguindigue S.S., and Cook P.F. Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction Biochemistry 44 2005 5541 5550
    • (2005) Biochemistry , vol.44 , pp. 5541-5550
    • Rabeh, W.M.1    Alguindigue, S.S.2    Cook, P.F.3
  • 25
    • 33646581753 scopus 로고    scopus 로고
    • Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli
    • Zhao C., Kumada Y., Imanaka H., Imamura K., and Nakanishi K. Cloning, overexpression, purification, and characterization of O-acetylserine sulfhydrylase-B from Escherichia coli Protein Expr. Purif. 47 2006 607 613
    • (2006) Protein Expr. Purif. , vol.47 , pp. 607-613
    • Zhao, C.1    Kumada, Y.2    Imanaka, H.3    Imamura, K.4    Nakanishi, K.5
  • 26
    • 0033616977 scopus 로고    scopus 로고
    • Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1
    • 145-152
    • Kawarabayasi, Y., Hino, Y., Horikawa, H., Yamazaki, S., Haikawa, Y., Jin-no, K. et al. (1999). Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1. DNA Res. 6, 83-101, 145-152.
    • (1999) DNA Res. , vol.6 , pp. 83-101
    • Kawarabayasi, Y.1    Hino, Y.2    Horikawa, H.3    Yamazaki, S.4    Haikawa, Y.5    Jinno, K.6
  • 27
    • 0037377836 scopus 로고    scopus 로고
    • Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1
    • Mino K., and Ishikawa K. Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1 J. Bacteriol. 185 2003 2277 2284
    • (2003) J. Bacteriol. , vol.185 , pp. 2277-2284
    • Mino, K.1    Ishikawa, K.2
  • 28
    • 0142134254 scopus 로고    scopus 로고
    • A novel O-phospho-l-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1
    • Mino K., and Ishikawa K. A novel O-phospho-l-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1 FEBS Lett. 551 2003 133 138
    • (2003) FEBS Lett. , vol.551 , pp. 133-138
    • Mino, K.1    Ishikawa, K.2
  • 29
    • 75349089381 scopus 로고    scopus 로고
    • New function and application of the cysteine synthase from archaea
    • Ishikawa K., Mino K., and Nakamura T. New function and application of the cysteine synthase from archaea Biochem. Eng. J. 48 2010 315 322
    • (2010) Biochem. Eng. J. , vol.48 , pp. 315-322
    • Ishikawa, K.1    Mino, K.2    Nakamura, T.3
  • 30
    • 22444433528 scopus 로고    scopus 로고
    • Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 Å resolution
    • Oda Y., Mino K., Ishikawa K., and Ataka M. Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 Å resolution J. Mol. Biol. 351 2005 334 344
    • (2005) J. Mol. Biol. , vol.351 , pp. 334-344
    • Oda, Y.1    Mino, K.2    Ishikawa, K.3    Ataka, M.4
  • 31
    • 0031978286 scopus 로고    scopus 로고
    • Clinical and microbiological aspects of Trichomonas vaginalis
    • Petrin D., Delgaty K., Bhatt R., and Garber G. Clinical and microbiological aspects of Trichomonas vaginalis Clin. Microbiol. Rev. 11 1998 300 317
    • (1998) Clin. Microbiol. Rev. , vol.11 , pp. 300-317
    • Petrin, D.1    Delgaty, K.2    Bhatt, R.3    Garber, G.4
  • 32
    • 33846503255 scopus 로고    scopus 로고
    • Current therapeutics, their problems, and sulfur-containing-amino-acid metabolism as a novel target against infections by amitochondriate protozoan parasites
    • Ali V., and Nozaki T. Current therapeutics, their problems, and sulfur-containing-amino-acid metabolism as a novel target against infections by amitochondriate protozoan parasites Clin. Microbiol. Rev. 20 2007 164 187
    • (2007) Clin. Microbiol. Rev. , vol.20 , pp. 164-187
    • Ali, V.1    Nozaki, T.2
  • 35
    • 0017281552 scopus 로고
    • A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2
    • Cook P.F., and Wedding R.T. A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 J. Biol. Chem. 251 1976 2023 2029
    • (1976) J. Biol. Chem. , vol.251 , pp. 2023-2029
    • Cook, P.F.1    Wedding, R.T.2
  • 36
    • 0027183564 scopus 로고
    • Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Tai C.H., Nalabolu S.R., Jacobson T.M., Minter D.E., and Cook P.F. Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants Biochemistry 32 1993 6433 6442
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 37
    • 0029844625 scopus 로고    scopus 로고
    • A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst
    • Rege V.D., Kredich N.M., Tai C.H., Karsten W.E., Schnackerz K.D., and Cook P.F. A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst Biochemistry 35 1996 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
  • 38
    • 77954823582 scopus 로고    scopus 로고
    • Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A
    • Tian H., Guan R., Salsi E., Campanini B., Bettati S., and Kumar V.P. Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A Biochemistry 49 2010 6093 6103
    • (2010) Biochemistry , vol.49 , pp. 6093-6103
    • Tian, H.1    Guan, R.2    Salsi, E.3    Campanini, B.4    Bettati, S.5    Kumar, V.P.6
  • 39
    • 78650577404 scopus 로고    scopus 로고
    • NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes
    • Goroncy A.K., Murayama K., Shirouzu M., Kuramitsu S., Kigawa T., and Yokoyama S. NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes J. Struct. Funct. Genomics 11 2010 247 256
    • (2010) J. Struct. Funct. Genomics , vol.11 , pp. 247-256
    • Goroncy, A.K.1    Murayama, K.2    Shirouzu, M.3    Kuramitsu, S.4    Kigawa, T.5    Yokoyama, S.6
  • 40
    • 17644423923 scopus 로고    scopus 로고
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
    • Huang B., Vetting M.W., and Roderick S.L. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase J. Bacteriol. 187 2005 3201 3205
    • (2005) J. Bacteriol. , vol.187 , pp. 3201-3205
    • Huang, B.1    Vetting, M.W.2    Roderick, S.L.3
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Macromol. Crystallogr., Pt A 276 1997 307 326
    • (1997) Macromol. Crystallogr., Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 46
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde M.K. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids Biochem. J. 104 1967 627 633
    • (1967) Biochem. J. , vol.104 , pp. 627-633
    • Gaitonde, M.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.