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Volumn 134, Issue 2, 2003, Pages 307-314

Purification and characterization of aspartate racemase from the bivalve mollusk Scapharca broughtonii

Author keywords

Aspartate racemase; Blood shell; D Aspartate; L Aspartate; Pyridoxal 5 phosphate; Scapharca broughtonii

Indexed keywords

ALANINE; AMINOOXYACETIC ACID; ASPARTATE RACEMASE; ASPARTIC ACID; DEXTRO ASPARTIC ACID; GLUTAMIC ACID; PYRIDOXAL 5 PHOSPHATE; SERINE;

EID: 0037306393     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-4959(02)00267-1     Document Type: Article
Times cited : (53)

References (31)
  • 1
    • 0021183166 scopus 로고
    • Determination of D- and L-aspartate in amino acids mixtures by high-performance liquid chromatography after derivatization with a chiral adduct of o-phthalaldehyde
    • Aswad D.D. Determination of D- and L-aspartate in amino acids mixtures by high-performance liquid chromatography after derivatization with a chiral adduct of o-phthalaldehyde. Anal. Biochem. 137:1984;405-409.
    • (1984) Anal. Biochem. , vol.137 , pp. 405-409
    • Aswad, D.D.1
  • 2
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs G.E., Haldane J.B.S. A note on the kinetics of enzyme action. Biochem. J. 19:1925;338-339.
    • (1925) Biochem. J. , vol.19 , pp. 338-339
    • Briggs, G.E.1    Haldane, J.B.S.2
  • 3
    • 49149140032 scopus 로고
    • Presence of D-alanine in crustacean muscle and hepatopancreas
    • D'Aniello A., Giuditta A. Presence of D-alanine in crustacean muscle and hepatopancreas. Comp. Biochem. Physiol. Part B. 66:1980;319-322.
    • (1980) Comp. Biochem. Physiol. Part B , vol.66 , pp. 319-322
    • D'Aniello, A.1    Giuditta, A.2
  • 4
    • 0034601688 scopus 로고    scopus 로고
    • Human serine racemase: Molecular cloning, genomic organization and functional analysis
    • De Miranda J., Santoro A., Engelender S., Wolosker H. Human serine racemase: molecular cloning, genomic organization and functional analysis. Gene. 256:2000;183-188.
    • (2000) Gene , vol.256 , pp. 183-188
    • De Miranda, J.1    Santoro, A.2    Engelender, S.3    Wolosker, H.4
  • 5
    • 0022536214 scopus 로고
    • Biosynthetic alanine racemase of Salmonella typhimurium: Purification and characterization of the enzyme encoded by the alr gene
    • Esaki N., Walsh T. Biosynthetic alanine racemase of Salmonella typhimurium: purification and characterization of the enzyme encoded by the alr gene. Biochemistry. 25:1986;3261-3267.
    • (1986) Biochemistry , vol.25 , pp. 3261-3267
    • Esaki, N.1    Walsh, T.2
  • 6
    • 84993869094 scopus 로고
    • Occurrence and metabolism of D-aspartate in the gutless bivalve Solemya reidi
    • Felbeck H. Occurrence and metabolism of D-aspartate in the gutless bivalve Solemya reidi. J. Exp. Zool. 234:1985;145-149.
    • (1985) J. Exp. Zool. , vol.234 , pp. 145-149
    • Felbeck, H.1
  • 7
    • 0030850891 scopus 로고    scopus 로고
    • Free D-aspartate and D-serine in the mammalian brain and periphery
    • Hashimoto A., Oka T. Free D-aspartate and D-serine in the mammalian brain and periphery. Prog. Neurobiol. 52:1997;325-353.
    • (1997) Prog. Neurobiol. , vol.52 , pp. 325-353
    • Hashimoto, A.1    Oka, T.2
  • 8
    • 0022452427 scopus 로고
    • Thermostable alanine racemase from Bacillus stearothermophilus: Molecular cloning of the gene, enzyme purification and characterization
    • Inagaki K., Tanizawa K., Badet B., Walsh C.T., Tanaka H., Soda K. Thermostable alanine racemase from Bacillus stearothermophilus: molecular cloning of the gene, enzyme purification and characterization. Biochemistry. 25:1986;3268-3274.
    • (1986) Biochemistry , vol.25 , pp. 3268-3274
    • Inagaki, K.1    Tanizawa, K.2    Badet, B.3    Walsh, C.T.4    Tanaka, H.5    Soda, K.6
  • 9
    • 0032579989 scopus 로고    scopus 로고
    • Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium Pyrococcus horikoshii OT3
    • Kawarabayasi Y., Sawada M., Horikawa H., et al. Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium Pyrococcus horikoshii OT3. DNA Res. 5:1998;55-76.
    • (1998) DNA Res. , vol.5 , pp. 55-76
    • Kawarabayasi, Y.1    Sawada, M.2    Horikawa, H.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0034808464 scopus 로고    scopus 로고
    • Occurrence of D-amino acids and a pyridoxal 5′-phosphate-dependent aspartate racemase in the acidothermophilic archaeon, Thermoplasma acidophilum
    • Long Z., Lee J.A., Okamoto T., et al. Occurrence of D-amino acids and a pyridoxal 5′-phosphate-dependent aspartate racemase in the acidothermophilic archaeon, Thermoplasma acidophilum. Biochem. Biophys. Res. Commun. 281:2001;317-321.
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 317-321
    • Long, Z.1    Lee, J.A.2    Okamoto, T.3
  • 13
    • 0032692877 scopus 로고    scopus 로고
    • Occurrence of free D-amino acids and aspartate racemases in hyperthermophilic archaea
    • Matsumoto M., Homma H., Long Z., et al. Occurrence of free D-amino acids and aspartate racemases in hyperthermophilic archaea. J. Bacteriol. 181:1999;6560-6563.
    • (1999) J. Bacteriol. , vol.181 , pp. 6560-6563
    • Matsumoto, M.1    Homma, H.2    Long, Z.3
  • 14
    • 0035133965 scopus 로고    scopus 로고
    • Purification and some properties of alanine racemase from a bivalve mollusc Corbicula japonica
    • Nomura T., Yamamoto I., Morishita F., Furukawa Y., Matsushima O. Purification and some properties of alanine racemase from a bivalve mollusc Corbicula japonica. J. Exp. Zool. 289:2001;1-9.
    • (2001) J. Exp. Zool. , vol.289 , pp. 1-9
    • Nomura, T.1    Yamamoto, I.2    Morishita, F.3    Furukawa, Y.4    Matsushima, O.5
  • 16
    • 85011247264 scopus 로고
    • Distribution of free D-amino acids in the tissues of crustaceans
    • Okuma E., Fujita E., Amano H., Noda H., Abe H. Distribution of free D-amino acids in the tissues of crustaceans. Fish. Sci. 61:1995;157-160.
    • (1995) Fish. Sci. , vol.61 , pp. 157-160
    • Okuma, E.1    Fujita, E.2    Amano, H.3    Noda, H.4    Abe, H.5
  • 17
    • 0021769545 scopus 로고
    • Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D- and L-β-substituted alanines: Kinetics, stoichiometry, active site peptide, and mechanistic studies
    • Roise D., Soda K., Yagi T., Walsh C. Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D- and L-β-substituted alanines: kinetics, stoichiometry, active site peptide, and mechanistic studies. Biochemistry. 23:1984;5195-5201.
    • (1984) Biochemistry , vol.23 , pp. 5195-5201
    • Roise, D.1    Soda, K.2    Yagi, T.3    Walsh, C.4
  • 18
    • 0000962307 scopus 로고    scopus 로고
    • Alanine racemase from an acidophile, Acidiphilium organovorum: Purification and characterization
    • Seow T.K., Inagaki K., Tamura T., Soda K., Tanaka H. Alanine racemase from an acidophile, Acidiphilium organovorum: purification and characterization. Biosci. Biotechnol. Biochem. 62:1998;242-247.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 242-247
    • Seow, T.K.1    Inagaki, K.2    Tamura, T.3    Soda, K.4    Tanaka, H.5
  • 20
    • 0035961604 scopus 로고    scopus 로고
    • Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon
    • Uo T., Ueda M., Nishiyama T., Yoshimura T., Esaki N. Purification and characterization of alanine racemase from hepatopancreas of black-tiger prawn, Penaeus monodon. J. Mol. Catal. B. 12:2001;137-144.
    • (2001) J. Mol. Catal. B , vol.12 , pp. 137-144
    • Uo, T.1    Ueda, M.2    Nishiyama, T.3    Yoshimura, T.4    Esaki, N.5
  • 21
    • 0031827219 scopus 로고    scopus 로고
    • Occurrence of free D-aspartate and aspartate racemase in the blood shell Scapharca broughtonii
    • Watanabe T., Shibata K., Kera Y., Yamada R. Occurrence of free D-aspartate and aspartate racemase in the blood shell Scapharca broughtonii. Amino Acids. 14:1998;353-360.
    • (1998) Amino Acids , vol.14 , pp. 353-360
    • Watanabe, T.1    Shibata, K.2    Kera, Y.3    Yamada, R.4
  • 22
    • 0033582230 scopus 로고    scopus 로고
    • Purification of serine racemase: Biosynthesis of the neuromodulator of D-serine
    • Wolosker H., Sheth K.N., Takahashi M., et al. Purification of serine racemase: biosynthesis of the neuromodulator of D-serine. Proc. Natl. Acad. Sci. USA. 96:1999a;721-725.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 721-725
    • Wolosker, H.1    Sheth, K.N.2    Takahashi, M.3
  • 23
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: A glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission
    • Wolosker H., Blackshaw S., Snyder S.H. Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission. Proc. Natl. Acad. Sci. USA. 96:1999b;13409-13414.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13409-13414
    • Wolosker, H.1    Blackshaw, S.2    Snyder, S.H.3
  • 24
    • 0034618848 scopus 로고    scopus 로고
    • D-Aspartate disposition in neuronal and endocrine tissues: Ontogeny, biosynthesis and release
    • Wolosker H., D'Aniello A., Snyder S.H. D-Aspartate disposition in neuronal and endocrine tissues: ontogeny, biosynthesis and release. Neuroscience. 100:2000;183-189.
    • (2000) Neuroscience , vol.100 , pp. 183-189
    • Wolosker, H.1    D'Aniello, A.2    Snyder, S.H.3
  • 25
    • 0026471651 scopus 로고
    • The relation of D-alanine and alanine racemase activity in molluscs
    • Yamada A., Matsushima O. The relation of D-alanine and alanine racemase activity in molluscs. Comp. Biochem. Physiol. Part B. 103:1992;617-621.
    • (1992) Comp. Biochem. Physiol. Part B , vol.103 , pp. 617-621
    • Yamada, A.1    Matsushima, O.2
  • 26
    • 0029936956 scopus 로고    scopus 로고
    • Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ I
    • Yamada R., Ujiie H., Kera Y., et al. Purification and properties of D-aspartate oxidase from Cryptococcus humicolus UJ I. Biochim. Biophys. Acta. 1294:1996;153-158.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 153-158
    • Yamada, R.1    Ujiie, H.2    Kera, Y.3
  • 27
    • 0026655552 scopus 로고
    • Properties of aspartate racemase, a pyridoxal 5′-phosphate-independent amino acid racemase
    • Yamauchi T., Choi S.Y., Okada H., et al. Properties of aspartate racemase, a pyridoxal 5′-phosphate-independent amino acid racemase. J. Biol. Chem. 267:1992;18361-18364.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18361-18364
    • Yamauchi, T.1    Choi, S.Y.2    Okada, H.3
  • 28
    • 0027342433 scopus 로고
    • Thermolabile alanine racemase from a psychrotroph, Pseudomonas fluorescens: Purification and properties
    • Yokoigawa K., Kawai H., Endo K., Lim Y.H., Esaki N., Soda K. Thermolabile alanine racemase from a psychrotroph, Pseudomonas fluorescens: purification and properties. Biosci. Biotechnol. Biochem. 57:1993;93-97.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 93-97
    • Yokoigawa, K.1    Kawai, H.2    Endo, K.3    Lim, Y.H.4    Esaki, N.5    Soda, K.6
  • 29
    • 0029811103 scopus 로고    scopus 로고
    • Gene for aspartate racemase from the sulfur-dependent hyperthermophilic archaeum, Desulfurococcus strain SY
    • Yohda M., Endo I., Abe Y., et al. Gene for aspartate racemase from the sulfur-dependent hyperthermophilic archaeum, Desulfurococcus strain SY. J. Biol. Chem. 271:1996;22017-22021.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22017-22021
    • Yohda, M.1    Endo, I.2    Abe, Y.3
  • 31
    • 0036848173 scopus 로고    scopus 로고
    • Purification, properties, and partial amino acid sequences of alanine racemase from the muscle of the black tiger prawn Penaeus monodon
    • Yoshikawa N., Dhomae N., Koji T., Abe H. Purification, properties, and partial amino acid sequences of alanine racemase from the muscle of the black tiger prawn Penaeus monodon. Comp. Biochem. Physiol. Part B. 133:2002;445-453.
    • (2002) Comp. Biochem. Physiol. Part B , vol.133 , pp. 445-453
    • Yoshikawa, N.1    Dhomae, N.2    Koji, T.3    Abe, H.4


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