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Volumn 7, Issue 5, 2012, Pages

Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase

Author keywords

[No Author keywords available]

Indexed keywords

1 AMINO A CARBOXY CYCLOPROPANE; 3 CHLORO DEXTRO ALANINE; ALANINE DERIVATIVE; CYCLOPROPANE DERIVATIVE; CYCLOSERINE; CYSTATHIONINE GAMMA LYASE; DEXTRO SERINE; LIGAND; POLYPEPTIDE; PYRIDOXAL 5 PHOSPHATE; PYRIDOXAMINE PHOSPHATE; PYRUVIC ACID; SERINE; TYROSINE; UNCLASSIFIED DRUG; 1 AMINOCYCLOPROPANECARBOXYLIC ACID; 1-AMINOCYCLOPROPANE-1-CARBOXYLIC ACID; 3 CHLOROALANINE; 3-CHLOROALANINE; AMINO ACID; BETA ALANINE; DRUG DERIVATIVE;

EID: 84860530513     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036267     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 9744235147 scopus 로고    scopus 로고
    • Reaction specificity in pyridoxal phosphate enzymes
    • Toney MD, (2005) Reaction specificity in pyridoxal phosphate enzymes. Arch Biochem Biophys 433: 279-287.
    • (2005) Arch Biochem Biophys , vol.433 , pp. 279-287
    • Toney, M.D.1
  • 2
    • 0028044574 scopus 로고
    • Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families
    • Alexander FW, Sandmeier E, Mehta PK, Christen P, (1994) Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families. Eur J Biochem 219: 953-960.
    • (1994) Eur J Biochem , vol.219 , pp. 953-960
    • Alexander, F.W.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4
  • 3
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • Jansonius JN, (1998) Structure, evolution and action of vitamin B6-dependent enzymes. Curr Opin Struct Biol 8: 759-769.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 4
    • 79961027797 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of d-serine deaminase from Salmonella typhimurium - implications on substrate specificity and catalysis
    • Bharath SR, Bisht S, Savithri HS, Murthy MR, (2011) Crystal structures of open and closed forms of d-serine deaminase from Salmonella typhimurium- implications on substrate specificity and catalysis. FEBS J 278: 2879-2891.
    • (2011) FEBS J , vol.278 , pp. 2879-2891
    • Bharath, S.R.1    Bisht, S.2    Savithri, H.S.3    Murthy, M.R.4
  • 5
    • 0021750407 scopus 로고
    • In vitro and in vivo antibacterial activities of MT-141, a new semisynthetic cephamycin, compared with those of five cephalosporins
    • Inouye S, Goi H, Watanabe T, Hara T, Miyauchi K, et al. (1984) In vitro and in vivo antibacterial activities of MT-141, a new semisynthetic cephamycin, compared with those of five cephalosporins. Antimicrob Agents Chemother 26: 722-729.
    • (1984) Antimicrob Agents Chemother , vol.26 , pp. 722-729
    • Inouye, S.1    Goi, H.2    Watanabe, T.3    Hara, T.4    Miyauchi, K.5
  • 6
    • 0021739579 scopus 로고
    • Structure-activity relationships on the terminal D-amino acid moiety of a novel cephamycin MT-141
    • Inouye S, Tsuruoka T, Goi H, Iwamatsu K, Miyauchi K, et al. (1984) Structure-activity relationships on the terminal D-amino acid moiety of a novel cephamycin MT-141. J Antibiot (Tokyo) 37: 1403-1413.
    • (1984) J Antibiot (Tokyo) , vol.37 , pp. 1403-1413
    • Inouye, S.1    Tsuruoka, T.2    Goi, H.3    Iwamatsu, K.4    Miyauchi, K.5
  • 7
    • 0022311120 scopus 로고
    • D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization
    • Nagasawa T, Ishii T, Kumagai H, Yamada H, (1985) D-Cysteine desulfhydrase of Escherichia coli. Purification and characterization. Eur J Biochem 153: 541-551.
    • (1985) Eur J Biochem , vol.153 , pp. 541-551
    • Nagasawa, T.1    Ishii, T.2    Kumagai, H.3    Yamada, H.4
  • 8
    • 0032522653 scopus 로고    scopus 로고
    • Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase
    • Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, et al. (1998) Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. Structure 6: 465-475.
    • (1998) Structure , vol.6 , pp. 465-475
    • Gallagher, D.T.1    Gilliland, G.L.2    Xiao, G.3    Zondlo, J.4    Fisher, K.E.5
  • 9
    • 0242507490 scopus 로고    scopus 로고
    • Crystal structure of serine dehydratase from rat liver
    • Yamada T, Komoto J, Takata Y, Ogawa H, Pitot HC, et al. (2003) Crystal structure of serine dehydratase from rat liver. Biochemistry 42: 12854-12865.
    • (2003) Biochemistry , vol.42 , pp. 12854-12865
    • Yamada, T.1    Komoto, J.2    Takata, Y.3    Ogawa, H.4    Pitot, H.C.5
  • 10
    • 33845991866 scopus 로고    scopus 로고
    • Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation
    • Simanshu DK, Savithri HS, Murthy MR, (2006) Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation. J Biol Chem 281: 39630-39641.
    • (2006) J Biol Chem , vol.281 , pp. 39630-39641
    • Simanshu, D.K.1    Savithri, H.S.2    Murthy, M.R.3
  • 11
    • 0027247728 scopus 로고
    • Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters
    • Grabowski R, Hofmeister AE, Buckel W, (1993) Bacterial L-serine dehydratases: a new family of enzymes containing iron-sulfur clusters. Trends Biochem Sci 18: 297-300.
    • (1993) Trends Biochem Sci , vol.18 , pp. 297-300
    • Grabowski, R.1    Hofmeister, A.E.2    Buckel, W.3
  • 12
    • 0034602162 scopus 로고    scopus 로고
    • Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus
    • Yao M, Ose T, Sugimoto H, Horiuchi A, Nakagawa A, et al. (2000) Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus. J Biol Chem 275: 34557-34565.
    • (2000) J Biol Chem , vol.275 , pp. 34557-34565
    • Yao, M.1    Ose, T.2    Sugimoto, H.3    Horiuchi, A.4    Nakagawa, A.5
  • 13
    • 6344228463 scopus 로고    scopus 로고
    • Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5′-phosphate dependent cyclopropane ring-opening reaction
    • Karthikeyan S, Zhou Q, Zhao Z, Kao CL, Tao Z, et al. (2004) Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5′-phosphate dependent cyclopropane ring-opening reaction. Biochemistry 43: 13328-13339.
    • (2004) Biochemistry , vol.43 , pp. 13328-13339
    • Karthikeyan, S.1    Zhou, Q.2    Zhao, Z.3    Kao, C.L.4    Tao, Z.5
  • 14
    • 3843053555 scopus 로고    scopus 로고
    • Structural and enzymatic properties of 1-aminocyclopropane-1-carboxylate deaminase homologue from Pyrococcus horikoshii
    • Fujino A, Ose T, Yao M, Tokiwano T, Honma M, et al. (2004) Structural and enzymatic properties of 1-aminocyclopropane-1-carboxylate deaminase homologue from Pyrococcus horikoshii. J Mol Biol 341: 999-1013.
    • (2004) J Mol Biol , vol.341 , pp. 999-1013
    • Fujino, A.1    Ose, T.2    Yao, M.3    Tokiwano, T.4    Honma, M.5
  • 15
    • 0142039869 scopus 로고    scopus 로고
    • Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction
    • Ose T, Fujino A, Yao M, Watanabe N, Honma M, et al. (2003) Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction. J Biol Chem 278: 41069-41076.
    • (2003) J Biol Chem , vol.278 , pp. 41069-41076
    • Ose, T.1    Fujino, A.2    Yao, M.3    Watanabe, N.4    Honma, M.5
  • 18
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 19
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 20
    • 0024297340 scopus 로고
    • Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium
    • Hyde CC, Ahmed SA, Padlan EA, Miles EW, Davies DR, (1988) Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium. J Biol Chem 263: 17857-17871.
    • (1988) J Biol Chem , vol.263 , pp. 17857-17871
    • Hyde, C.C.1    Ahmed, S.A.2    Padlan, E.A.3    Miles, E.W.4    Davies, D.R.5
  • 21
    • 0344157394 scopus 로고    scopus 로고
    • Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, et al. (1998) Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. J Mol Biol 283: 121-133.
    • (1998) J Mol Biol , vol.283 , pp. 121-133
    • Burkhard, P.1    Rao, G.S.2    Hohenester, E.3    Schnackerz, K.D.4    Cook, P.F.5
  • 22
    • 34249111417 scopus 로고    scopus 로고
    • NMR studies of coupled low- and high-barrier hydrogen bonds in pyridoxal-5′-phosphate model systems in polar solution
    • Sharif S, Denisov GS, Toney MD, Limbach HH, (2007) NMR studies of coupled low- and high-barrier hydrogen bonds in pyridoxal-5′-phosphate model systems in polar solution. J Am Chem Soc 129: 6313-6327.
    • (2007) J Am Chem Soc , vol.129 , pp. 6313-6327
    • Sharif, S.1    Denisov, G.S.2    Toney, M.D.3    Limbach, H.H.4
  • 23
    • 56649118960 scopus 로고    scopus 로고
    • The interconversion of ACC deaminase and D-cysteine desulfhydrase by directed mutagenesis
    • Todorovic B, Glick BR, (2008) The interconversion of ACC deaminase and D-cysteine desulfhydrase by directed mutagenesis. Planta 229: 193-205.
    • (2008) Planta , vol.229 , pp. 193-205
    • Todorovic, B.1    Glick, B.R.2
  • 24
    • 33847142225 scopus 로고    scopus 로고
    • CAVER: a new tool to explore routes from protein clefts, pockets and cavities
    • Petrek M, Otyepka M, Banas P, Kosinova P, Koca J, et al. (2006) CAVER: a new tool to explore routes from protein clefts, pockets and cavities. BMC Bioinformatics 7: 316.
    • (2006) BMC Bioinformatics , vol.7 , pp. 316
    • Petrek, M.1    Otyepka, M.2    Banas, P.3    Kosinova, P.4    Koca, J.5
  • 25
    • 67849130559 scopus 로고    scopus 로고
    • HotSpot Wizard: a web server for identification of hot spots in protein engineering
    • Pavelka A, Chovancova E, Damborsky J, (2009) HotSpot Wizard: a web server for identification of hot spots in protein engineering. Nucleic Acids Res 37: W376-383.
    • (2009) Nucleic Acids Res , vol.37
    • Pavelka, A.1    Chovancova, E.2    Damborsky, J.3
  • 26
    • 0021099511 scopus 로고
    • A reaction pathway for transimination of the pyridoxal 5′-phosphate in D-serine dehydratase by amino acids
    • Federiuk CS, Shafer JA, (1983) A reaction pathway for transimination of the pyridoxal 5′-phosphate in D-serine dehydratase by amino acids. J Biol Chem 258: 5372-5378.
    • (1983) J Biol Chem , vol.258 , pp. 5372-5378
    • Federiuk, C.S.1    Shafer, J.A.2
  • 27
    • 0942290628 scopus 로고    scopus 로고
    • Reactions of serine palmitoyltransferase with serine and molecular mechanisms of the actions of serine derivatives as inhibitors
    • Ikushiro H, Hayashi H, Kagamiyama H, (2004) Reactions of serine palmitoyltransferase with serine and molecular mechanisms of the actions of serine derivatives as inhibitors. Biochemistry 43: 1082-1092.
    • (2004) Biochemistry , vol.43 , pp. 1082-1092
    • Ikushiro, H.1    Hayashi, H.2    Kagamiyama, H.3
  • 28
    • 0018784025 scopus 로고
    • Mechanism of action of D-serine dehydratase. Identification of a transient intermediate
    • Schnackerz KD, Ehrlich JH, Giesemann W, Reed TA, (1979) Mechanism of action of D-serine dehydratase. Identification of a transient intermediate. Biochemistry 18: 3557-3563.
    • (1979) Biochemistry , vol.18 , pp. 3557-3563
    • Schnackerz, K.D.1    Ehrlich, J.H.2    Giesemann, W.3    Reed, T.A.4
  • 29
    • 70350035997 scopus 로고    scopus 로고
    • Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe
    • Goto M, Yamauchi T, Kamiya N, Miyahara I, Yoshimura T, et al. (2009) Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe. J Biol Chem 284: 25944-25952.
    • (2009) J Biol Chem , vol.284 , pp. 25944-25952
    • Goto, M.1    Yamauchi, T.2    Kamiya, N.3    Miyahara, I.4    Yoshimura, T.5
  • 30
    • 77951223140 scopus 로고    scopus 로고
    • The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding
    • Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, et al. (2010) The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem 285: 12873-12881.
    • (2010) J Biol Chem , vol.285 , pp. 12873-12881
    • Smith, M.A.1    Mack, V.2    Ebneth, A.3    Moraes, I.4    Felicetti, B.5
  • 31
    • 77956901490 scopus 로고
    • In: Boyer PD, editors, The Enzymes: Academic press, New York
    • Davis L, Metzler DE, (1972) pp. 33-74 The Enzymes: Academic press, New York.
    • (1972) , pp. 33-74
    • Davis, L.1    Metzler, D.E.2
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology 276: 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4, (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 34
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions
    • Cohen GE, (1997) ALIGN: a program to superimpose protein coordinates, accounting for insertions and deletions. Journal of Applied Crystallography 30: 1160-1161.
    • (1997) Journal of Applied Crystallography , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 35
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 0038167027 scopus 로고    scopus 로고
    • Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA
    • Shenoy AR, Visweswariah SS, (2003) Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA. Anal Biochem 319: 335-336.
    • (2003) Anal Biochem , vol.319 , pp. 335-336
    • Shenoy, A.R.1    Visweswariah, S.S.2
  • 39
    • 38749092616 scopus 로고    scopus 로고
    • A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae
    • Ito T, Hemmi H, Kataoka K, Mukai Y, Yoshimura T, (2008) A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae. Biochem J 409: 399-406.
    • (2008) Biochem J , vol.409 , pp. 399-406
    • Ito, T.1    Hemmi, H.2    Kataoka, K.3    Mukai, Y.4    Yoshimura, T.5


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