메뉴 건너뛰기




Volumn 44, Issue 3, 2013, Pages 1073-1084

Catalytic mechanism of serine racemase from Dictyostelium discoideum

Author keywords

d serine; Dictyostelium discoideum; Pyridoxal 5 phosphate; Serine racemase

Indexed keywords

ALANINE; ALDIMINE; ALPHA HYDROGEN; CYSTEINE; DEHYDROALANINE; HYDROGEN; IMINE; PYRIDOXAL 5 PHOSPHATE; PYRUVIC ACID; QUINONE DERIVATIVE; RACEMASE; SERINE; SERINE DEHYDRATASE; SERINE RACEMASE; UNCLASSIFIED DRUG; WATER;

EID: 84878376335     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-012-1442-4     Document Type: Article
Times cited : (20)

References (27)
  • 1
    • 1242273640 scopus 로고    scopus 로고
    • Alpha, beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required?
    • 10.1016/S1570-9639(03)00052-9 12686110 10.1016/S1570-9639(03)00052-9 1:CAS:528:DC%2BD3sXislCjurg%3D
    • Cook PF (2003) Alpha, beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required? Biochim Biophys Acta 1647:66-69. doi: 10.1016/S1570-9639(03)00052-9
    • (2003) Biochim Biophys Acta , vol.1647 , pp. 66-69
    • Cook, P.F.1
  • 2
    • 0037195093 scopus 로고    scopus 로고
    • Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-d-aspartate (NMDA) receptor coagonist d-serine
    • 10.1073/pnas.222421299 12393813 10.1073/pnas.222421299
    • De Miranda J, Panizzutti R, Foltyn VN, Wolosker H (2002) Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-d-aspartate (NMDA) receptor coagonist d-serine. Proc Natl Acad Sci USA 99:14542-14547. doi: 10.1073/pnas.222421299
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14542-14547
    • De Miranda, J.1    Panizzutti, R.2    Foltyn, V.N.3    Wolosker, H.4
  • 3
    • 19944432442 scopus 로고    scopus 로고
    • Serine racemase modulates intracellular d-serine levels through an alpha, beta-elimination activity
    • 10.1074/jbc.M405726200 15536068 10.1074/jbc.M405726200 1:CAS:528:DC%2BD2MXksVSqtA%3D%3D
    • Foltyn VN, Bendikov I, De Miranda J, Panizzutti R, Dumin E, Shleper M, Li P, Toney MD, Kartvelishvily E, Wolosker H (2005) Serine racemase modulates intracellular d-serine levels through an alpha, beta-elimination activity. J Biol Chem 280:1754-1763. doi: 10.1074/jbc.M405726200
    • (2005) J Biol Chem , vol.280 , pp. 1754-1763
    • Foltyn, V.N.1    Bendikov, I.2    De Miranda, J.3    Panizzutti, R.4    Dumin, E.5    Shleper, M.6    Li, P.7    Toney, M.D.8    Kartvelishvily, E.9    Wolosker, H.10
  • 4
    • 70350035997 scopus 로고    scopus 로고
    • Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe
    • 10.1074/jbc.M109.010470 19640845 10.1074/jbc.M109.010470 1:CAS:528:DC%2BD1MXhtFWhtrzI
    • Goto M, Yamauchi T, Kamiya N, Miyahara I, Yoshimura T, Mihara H, Kurihara T, Hirotsu K, Esaki N (2009) Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe. J Biol Chem 284:25944-25952. doi: 10.1074/jbc.M109.010470
    • (2009) J Biol Chem , vol.284 , pp. 25944-25952
    • Goto, M.1    Yamauchi, T.2    Kamiya, N.3    Miyahara, I.4    Yoshimura, T.5    Mihara, H.6    Kurihara, T.7    Hirotsu, K.8    Esaki, N.9
  • 5
    • 80052819676 scopus 로고    scopus 로고
    • Role of the pyridine nitrogen in pyridoxal 5′-phosphate catalysis: Activity of three classes of PLP enzymes reconstituted with deazapyridoxal 5′-phosphate
    • 10.1021/ja2061006 21827189 10.1021/ja2061006 1:CAS:528:DC%2BC3MXhtVOns7rI
    • Griswold WR, Toney MD (2011) Role of the pyridine nitrogen in pyridoxal 5′-phosphate catalysis: activity of three classes of PLP enzymes reconstituted with deazapyridoxal 5′-phosphate. J Am Chem Soc 133:14823-14830. doi: 10.1021/ja2061006
    • (2011) J Am Chem Soc , vol.133 , pp. 14823-14830
    • Griswold, W.R.1    Toney, M.D.2
  • 6
    • 58149373550 scopus 로고    scopus 로고
    • NMDA- and beta-amyloid1-42-induced neurotoxicity is attenuated in serine racemase knock-out mice
    • 10.1523/JNEUROSCI.5034-08.2008 19118183 10.1523/JNEUROSCI.5034-08.2008 1:CAS:528:DC%2BD1MXnsF2ntA%3D%3D
    • Inoue R, Hashimoto K, Harai T, Mori H (2008) NMDA- and beta-amyloid1-42-induced neurotoxicity is attenuated in serine racemase knock-out mice. J Neurosci 28:14486-14491. doi: 10.1523/JNEUROSCI.5034-08.2008
    • (2008) J Neurosci , vol.28 , pp. 14486-14491
    • Inoue, R.1    Hashimoto, K.2    Harai, T.3    Mori, H.4
  • 7
    • 38749092616 scopus 로고    scopus 로고
    • A novel zinc-dependent d-serine dehydratase from Saccharomyces cerevisiae
    • 10.1042/BJ20070642 17937657 10.1042/BJ20070642 1:CAS:528: DC%2BD1cXhtlSrtbs%3D
    • 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. doi: 10.1042/BJ20070642
    • (2008) Biochem J. , vol.409 , pp. 399-406
    • Ito, T.1    Hemmi, H.2    Kataoka, K.3    Mukai, Y.4    Yoshimura, T.5
  • 8
    • 84867571648 scopus 로고    scopus 로고
    • Metal ion dependency of serine racemase from Dictyostelium discoideum
    • 10.1007/s00726-012-1232-z 22311068 10.1007/s00726-012-1232-z 1:CAS:528:DC%2BC38XhtlOlsrbM
    • Ito T, Murase H, Maekawa M, Goto M, Hayashi S, Saito H, Maki M, Hemmi H, Yoshimura T (2012a) Metal ion dependency of serine racemase from Dictyostelium discoideum. Amino Acids 43:1567-1576. doi: 10.1007/s00726-012-1232-z
    • (2012) Amino Acids , vol.43 , pp. 1567-1576
    • Ito, T.1    Murase, H.2    Maekawa, M.3    Goto, M.4    Hayashi, S.5    Saito, H.6    Maki, M.7    Hemmi, H.8    Yoshimura, T.9
  • 9
    • 84856330727 scopus 로고    scopus 로고
    • Role of zinc ion for catalytic activity in d-serine dehydratase from Saccharomyces cerevisiae
    • 10.1111/j.1742-4658.2011.08451.x 22176976 10.1111/j.1742-4658.2011.08451. x 1:CAS:528:DC%2BC38Xisleltro%3D
    • Ito T, Koga K, Hemmi H, Yoshimura T (2012b) Role of zinc ion for catalytic activity in d-serine dehydratase from Saccharomyces cerevisiae. FEBS J 279:612-624. doi: 10.1111/j.1742-4658.2011.08451.x
    • (2012) FEBS J , vol.279 , pp. 612-624
    • Ito, T.1    Koga, K.2    Hemmi, H.3    Yoshimura, T.4
  • 10
    • 33744900653 scopus 로고    scopus 로고
    • Neuron-derived d-serine release provides a novel means to activate N-methyl-d-aspartate receptors
    • 10.1074/jbc.M512927200 16551623 10.1074/jbc.M512927200 1:CAS:528:DC%2BD28XksFeisLo%3D
    • Kartvelishvily E, Shleper M, Balan L, Dumin E, Wolosker H (2006) Neuron-derived d-serine release provides a novel means to activate N-methyl-d-aspartate receptors. J Biol Chem 281:14151-14162. doi: 10.1074/jbc.M512927200
    • (2006) J Biol Chem , vol.281 , pp. 14151-14162
    • Kartvelishvily, E.1    Shleper, M.2    Balan, L.3    Dumin, E.4    Wolosker, H.5
  • 11
    • 0026504874 scopus 로고
    • Mechanism of racemization of amino acids by aspartate aminotransferase
    • 10.1111/j.1432-1033.1992.tb16584.x 1735441 10.1111/j.1432-1033.1992. tb16584.x 1:CAS:528:DyaK38XhsVKlur4%3D
    • Kochhar S, Christen P (1992) Mechanism of racemization of amino acids by aspartate aminotransferase. Eur J Biochem 203:563-569. doi: 10.1111/j.1432-1033. 1992.tb16584.x
    • (1992) Eur J Biochem , vol.203 , pp. 563-569
    • Kochhar, S.1    Christen, P.2
  • 12
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 10.1107/S0021889891004399 10.1107/S0021889891004399
    • Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950. doi: 10.1107/S0021889891004399
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 13
    • 0024522515 scopus 로고
    • The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230
    • 2495283 1:CAS:528:DyaL1MXhvVyntLc%3D
    • Miles EW, Kawasaki H, Ahmed SA, Morita H, Morita H, Nagata S (1989) The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230. J Biol Chem 264:6280-6287
    • (1989) J Biol Chem , vol.264 , pp. 6280-6287
    • Miles, E.W.1    Kawasaki, H.2    Ahmed, S.A.3    Morita, H.4    Morita, H.5    Nagata, S.6
  • 14
    • 77953898934 scopus 로고    scopus 로고
    • Serine racemase knockout mice
    • 10.1002/cbdv.200900293 20564570 10.1002/cbdv.200900293 1:CAS:528:DC%2BC3cXot1ansLs%3D
    • Mori H, Inoue R (2010) Serine racemase knockout mice. Chem Biodivers 7:1573-1578. doi: 10.1002/cbdv.200900293
    • (2010) Chem Biodivers , vol.7 , pp. 1573-1578
    • Mori, H.1    Inoue, R.2
  • 15
  • 16
    • 82555165853 scopus 로고    scopus 로고
    • Analysis of free d-serine in mammals and its biological relevance
    • 10.1016/j.jchromb.2011.08.030 21992750 10.1016/j.jchromb.2011.08.030 1:CAS:528:DC%2BC3MXhtlKrtb7O
    • Nishikawa T (2011) Analysis of free d-serine in mammals and its biological relevance. J Chromatogr B Analyt Technol Biomed Life Sci 879:3169-3183. doi: 10.1016/j.jchromb.2011.08.030
    • (2011) J Chromatogr B Analyt Technol Biomed Life Sci , vol.879 , pp. 3169-3183
    • Nishikawa, T.1
  • 17
    • 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
    • 10.1021/bi961517j 8873618 10.1021/bi961517j 1:CAS:528:DyaK28XlvVSlsLg%3D
    • Rege VD, Kredich NM, Tai CH, Karsten WE, Schnackerz KD, Cook PF (1996) 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 35:13485-13493. doi: 10.1021/bi961517j
    • (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
  • 18
    • 0031032448 scopus 로고    scopus 로고
    • Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution
    • 10.1021/bi961856c 9063881 10.1021/bi961856c 1:CAS:528: DyaK2sXmslOjuw%3D%3D
    • Shaw JP, Petsko GA, Ringe D (1997) Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-Å resolution. Biochemistry 36:1329-1342. doi: 10.1021/bi961856c
    • (1997) Biochemistry , vol.36 , pp. 1329-1342
    • Shaw, J.P.1    Petsko, G.A.2    Ringe, D.3
  • 19
    • 77951223140 scopus 로고    scopus 로고
    • The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding
    • 10.1074/jbc.M109.050062 20106978 10.1074/jbc.M109.050062 1:CAS:528:DC%2BC3cXkvVGju7c%3D
    • Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J (2010) The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding. J Biol Chem 285:12873-12881. doi: 10.1074/jbc.M109.050062
    • (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    Wood, M.6    Schonfeld, D.7    Mather, O.8    Cesura, A.9    Barker, J.10
  • 21
    • 0030606789 scopus 로고    scopus 로고
    • Time-resolved fluorescence of tryptophan synthase
    • 10.1016/0301-4622(96)00020-8 8855356 10.1016/0301-4622(96)00020-8 1:CAS:528:DyaK28XmtVartb8%3D
    • Vaccari S, Benci S, Peracchi A, Mozzarelli A (1996) Time-resolved fluorescence of tryptophan synthase. Biophys Chem 61:9-22. doi: 10.1016/0301-4622(96)00020-8
    • (1996) Biophys Chem , vol.61 , pp. 9-22
    • Vaccari, S.1    Benci, S.2    Peracchi, A.3    Mozzarelli, A.4
  • 22
    • 0033548158 scopus 로고    scopus 로고
    • Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5′-phosphate. Chemical rescue studies of Lys39- > Ala mutant
    • 10.1074/jbc.274.7.4189 9933615 10.1074/jbc.274.7.4189 1:STN:280:DyaK1M7jsVentA%3D%3D
    • Watanabe A, Kurokawa Y, Yoshimura T, Kurihara T, Soda K, Esaki N (1999) Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5′-phosphate. Chemical rescue studies of Lys39- > Ala mutant. J Biol Chem 274:4189-4194. doi: 10.1074/jbc.274.7.4189
    • (1999) J Biol Chem , vol.274 , pp. 4189-4194
    • Watanabe, A.1    Kurokawa, Y.2    Yoshimura, T.3    Kurihara, T.4    Soda, K.5    Esaki, N.6
  • 23
    • 0037166337 scopus 로고    scopus 로고
    • Reaction mechanism of alanine racemase from Bacillus stearothermophilus: X-ray crystallographic studies of the enzyme bound with N-(5′- phosphopyridoxyl)alanine
    • 10.1074/jbc.M201615200 11886871 10.1074/jbc.M201615200 1:CAS:528:DC%2BD38XktFChtbY%3D
    • Watanabe A, Yoshimura T, Mikami B, Hayashi H, Kagamiyama H, Esaki N (2002) Reaction mechanism of alanine racemase from Bacillus stearothermophilus: X-ray crystallographic studies of the enzyme bound with N-(5′- phosphopyridoxyl)alanine. J Biol Chem 277:19166-19172. doi: 10.1074/jbc. M201615200
    • (2002) J Biol Chem , vol.277 , pp. 19166-19172
    • Watanabe, A.1    Yoshimura, T.2    Mikami, B.3    Hayashi, H.4    Kagamiyama, H.5    Esaki, N.6
  • 24
    • 0033582230 scopus 로고    scopus 로고
    • Purification of serine racemase: Biosynthesis of the neuromodulator d-serine
    • 10.1073/pnas.96.2.721 9892700 10.1073/pnas.96.2.721 1:CAS:528: DyaK1MXmtlCrug%3D%3D
    • Wolosker H, Sheth KN, Takahashi M, Mothet JP, Brady RO Jr, Ferris CD, Snyder SH (1999) Purification of serine racemase: biosynthesis of the neuromodulator d-serine. Proc Natl Acad Sci USA 96:721-725. doi: 10.1073/pnas.96.2.721
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 721-725
    • Wolosker, H.1    Sheth, K.N.2    Takahashi, M.3    Mothet, J.P.4    Brady, Jr.R.O.5    Ferris, C.D.6    Snyder, S.H.7
  • 25
    • 0242507490 scopus 로고    scopus 로고
    • Crystal structure of serine dehydratase from rat liver
    • 10.1021/bi035324p 14596599 10.1021/bi035324p 1:CAS:528: DC%2BD3sXotFCgtr4%3D
    • Yamada T, Komoto J, Takata Y, Ogawa H, Pitot HC, Takusagawa F (2003) Crystal structure of serine dehydratase from rat liver. Biochemistry 42:12854-12865. doi: 10.1021/bi035324p
    • (2003) Biochemistry , vol.42 , pp. 12854-12865
    • Yamada, T.1    Komoto, J.2    Takata, Y.3    Ogawa, H.4    Pitot, H.C.5    Takusagawa, F.6
  • 27
    • 50549102620 scopus 로고    scopus 로고
    • D-amino acids in the brain: Structure and function of pyridoxal phosphate-dependent amino acid racemases
    • 10.1111/j.1742-4658.2008.06516.x 18564179 10.1111/j.1742-4658.2008.06516. x 1:CAS:528:DC%2BD1cXovVSmtLk%3D
    • Yoshimura T, Goto M (2008) D-amino acids in the brain: structure and function of pyridoxal phosphate-dependent amino acid racemases. FEBS J 275:3527-3537. doi: 10.1111/j.1742-4658.2008.06516.x
    • (2008) FEBS J , vol.275 , pp. 3527-3537
    • Yoshimura, T.1    Goto, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.