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Volumn 145, Issue 4, 2009, Pages 421-424

Serine racemase with catalytically active lysinoalanyl residue

Author keywords

D serine; Modification; Pyridoxal 5 phosphate; Racemase; Schizosaccharomyces pombe

Indexed keywords

BRAIN ENZYME; DEXTRO SERINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PYRIDOXAL 5 PHOSPHATE; RACEMASE; SCHIFF BASE; SERINE; ALANINE RACEMASE; ISOMERASE; LYSINOALANINE; SERINE RACEMASE;

EID: 67649670256     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp010     Document Type: Article
Times cited : (28)

References (14)
  • 2
    • 33750585899 scopus 로고    scopus 로고
    • D-Serine regulation of NMDA receptor activity
    • Wolosker, H. (2006) D-Serine regulation of NMDA receptor activity. Sci. STKE 356, 41
    • (2006) Sci. STKE , vol.356 , pp. 41
    • Wolosker, H.1
  • 3
    • 0037177552 scopus 로고    scopus 로고
    • Schizophrenia: Diverse approaches to a complex disease
    • Sawa, A. and Snyder, S. H. (2002) Schizophrenia: diverse approaches to a complex disease. Science 296, 692-695
    • (2002) Science , vol.296 , pp. 692-695
    • Sawa, A.1    Snyder, S.H.2
  • 4
    • 0037195093 scopus 로고    scopus 로고
    • Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-seine
    • de Miranda, J., Panizzutti, R., Foltyn, V.N., and Wolosker, H. (2002) Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-seine. Proc. Natl Acad. Sci. USA 99, 14542-14547
    • (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
  • 6
    • 0033539510 scopus 로고    scopus 로고
    • Serine racemase: A glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission
    • Wolosker, H.A., Blackshaw, S., and Snyder, S.H. (1999) Serine racemase: A glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission. Proc. Natl Acad. Sci. USA. 96, 13409-13414
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13409-13414
    • Wolosker, H.A.1    Blackshaw, S.2    Snyder, S.H.3
  • 7
    • 33846236550 scopus 로고    scopus 로고
    • Exploring the pyridoxal 5′-phosphate-dependent enzyme
    • Mozzarelli, A. and Bettati, S. (2006) Exploring the pyridoxal 5′-phosphate-dependent enzyme. Chem. Rec. 6, 275-287
    • (2006) Chem. Rec. , vol.6 , pp. 275-287
    • Mozzarelli, A.1    Bettati, S.2
  • 8
    • 0021769535 scopus 로고
    • Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of β-substituted alanines: Kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism
    • Badet, B., Roise, D., and Walsh, C.T. (1984) Inactivation of the dadB Salmonella typhimurium alanine racemase by D and L isomers of β-substituted alanines: kinetics, stoichiometry, active site peptide sequencing, and reaction mechanism. Biochemistry 23, 5188-5194
    • (1984) Biochemistry , vol.23 , pp. 5188-5194
    • Badet, B.1    Roise, D.2    Walsh, C.T.3
  • 9
    • 0022536214 scopus 로고
    • Biosynthetic alanine racemase of Salmonella typhimurium: Purification and characterization of the enzyme encoded by the alr gene
    • Esaki, N. and Walsh, C. T. (1986) Biosynthetic alanine racemase of Salmonella typhimurium: purification and characterization of the enzyme encoded by the alr gene. Biochemistry 25, 3261-3267
    • (1986) Biochemistry , vol.25 , pp. 3261-3267
    • Esaki, N.1    Walsh, C.T.2
  • 10
    • 0021769545 scopus 로고
    • Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of β-substituted alanines: Kinetics, stoichiometry, active site peptide, and mechanistic studies
    • Roise, D., Soda, K., Yagi, T., and Walsh, C.T. (1984) Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of β-substituted alanines: kinetics, stoichiometry, active site peptide, and mechanistic studies. Biochemistry 23, 5195-5201
    • (1984) Biochemistry , vol.23 , pp. 5195-5201
    • Roise, D.1    Soda, K.2    Yagi, T.3    Walsh, C.T.4
  • 11
    • 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. (1999) Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. J. Mol. Biol. 291, 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
  • 12
    • 0242495818 scopus 로고    scopus 로고
    • Crysral structures of threonine synthase from Thermus thermophilus HB8: Conformational change, substrate recognition, and mechanism
    • Omi, R., Goto, M., Miyahara, I., Mizuguchi, H., Hayashi, H., Kagamiyama, H., and Hirotsu, K. (2003) Crysral structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism. J. Biol. Chem. 278, 46035-46045
    • (2003) J. Biol. Chem. , vol.278 , pp. 46035-46045
    • Omi, R.1    Goto, M.2    Miyahara, I.3    Mizuguchi, H.4    Hayashi, H.5    Kagamiyama, H.6    Hirotsu, K.7
  • 13
    • 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
    • Watanabe, A., Yoshimura, T., Mikami, B., Hayashi, H., Kagamiyama, H., and 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
    • (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
  • 14
    • 0035942231 scopus 로고    scopus 로고
    • A new strategy to decreace N-methyl-D-aspartate (NMDA) receptor coactivation: Inhibition of D-serine synthesis by converting serine racemase into an eliminase
    • Panizzutti, R., De Miranda, J., Ribeiro, C., Engelender, S., and Wolosker, H. (2001) A new strategy to decreace N-methyl-D-aspartate (NMDA) receptor coactivation: inhibition of D-serine synthesis by converting serine racemase into an eliminase. Proc. Natl Acad. Sci. USA 98, 5294-5299
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5294-5299
    • Panizzutti, R.1    De Miranda, J.2    Ribeiro, C.3    Engelender, S.4    Wolosker, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.