Isolation and amino acid sequence of a dehydratase acting on d-erythro-3-hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate

References

• Perry TL, Jones RT. The amino acid content of human cerebrospinal fluid in normal individuals and in mental defectives. J Clin Invest. 1961;40:1363–1372.10.1172/JCI104367
   PubMed Web of Science ®Google Scholar
• Jenkins WT. Glutamic-aspartic transaminase VI. The reaction with certain β-substituted aspartic acid analogues. J Biol Chem. 1961;236:1121–1125.
   PubMed Web of Science ®Google Scholar
• Gibbs RG, Morris JG. Assay and properties of β-hydroxyaspartate aldolase from Micrococcus denitrificans. Biochim Biophys Acta. 1964;85:501–503.
   PubMed Web of Science ®Google Scholar
• Kornberg HL, Morris JG. The utilization of glycollate by Micrococcus denitrificans: the β-hydroxyaspartate pathway. Biochem J. 1965;95:577–586.10.1042/bj0950577
   PubMed Web of Science ®Google Scholar
• Grimwood S, Foster AC, Kemp JA. The pharmacological specificity of N-methyl-D-aspartate receptors in rat cerebral cortex: correspondence between radioligand binding and electrophysiological measurements. Br J Pharmacol. 1991;103:1385–1392.10.1111/bph.1991.103.issue-2
   PubMed Web of Science ®Google Scholar
• Shimamoto K. Glutamate transporter blockers for elucidation of the function of excitatory neurotransmission systems. Chem Rec. 2008;8:182–199.10.1002/(ISSN)1528-0691
   PubMed Web of Science ®Google Scholar
• Střísovšký K, Jirásková J, Mikulová A, et al. Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the β-eliminase activity. Biochemistry. 2005;44:13091–13100.
   PubMed Web of Science ®Google Scholar
• Saito S, Komada K, Moriwake T. Diethyl (2S,3R)-2-(N-tert-butoxycarbonyl)amino-3-hydroxysuccinate. Org Synth. 1996;73:184–191.
   Web of Science ®Google Scholar
• Cardillo G, Gentilucci L, Tolomelli A, et al. A practical method for the synthesis of β-amino α-hydroxy acids. synthesis of enantiomerically pure hydroxyaspartic acid and isoserine. Synlett. 1999;11:1727–1730.10.1055/s-1999-2927
   Web of Science ®Google Scholar
• Hanessian S, Vanasse B. Novel access to (3R)- and (3S)-3-hydroxy-L-aspartic acids, (4S)-4-hydroxy-L-glutamic acid, and related amino acids. Can J Chem. 1993;71:1401–1406.10.1139/v93-181
   Web of Science ®Google Scholar
• Kaneko T, Katsura H. The synthesis of four optical isomers of β-hydroxyaspartic acid. Bull Chem Soc Jpn. 1963;36:899–903.10.1246/bcsj.36.899
   Web of Science ®Google Scholar
• Matsumoto Y, Yasutake Y, Takeda Y, et al. Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate. Appl Microbiol Biotechnol. 2015;99:7137–7150.10.1007/s00253-015-6479-3
   PubMed Web of Science ®Google Scholar
• Maeda T, Takeda Y, Murakami T, et al. Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23. J Biochem. 2010;148:705–712.10.1093/jb/mvq106
   PubMed Web of Science ®Google Scholar
• Strieker M, Essen LO, Walsh CT, et al. Non-heme hydroxylase engineering for simple enzymatic synthesis of L-threo-hydroxyaspartic acid. ChemBioChem. 2008;9:374–376.10.1002/(ISSN)1439-7633
   PubMed Web of Science ®Google Scholar
• Hara R, Nakano M, Kino K. One-pot production of L-threo-3-hydroxyaspartic acid using asparaginase-deficient Escherichia coli expressing asparagine hydroxylase of Streptomyces coelicolor A3(2). Appl Environ Microbiol. 2015;81:3648–3654.10.1128/AEM.03963-14
   PubMed Web of Science ®Google Scholar
• Balcar VJ, Johnston GAR, Twitchin B. Stereospecificity of the inhibition of L-glutamate and L-aspartate high affinity uptake in rat brain slices by threo-3-hydroxyaspartate. J Neurochem. 1977;28:1145–1146.10.1111/jnc.1977.28.issue-5
   PubMed Web of Science ®Google Scholar
• Foster AC, Li YX, Runyan S, et al. Activity of the enantiomers of erythro-3-hydroxyaspartate at glutamate transporters and NMDA receptors. J Neurochem. 2016;136:692–697.
   PubMed Web of Science ®Google Scholar
• Wada M, Nakamori S, Takagi H. Serine racemase homologue of Saccharomyces cerevisiae has L-threo-3-hydroxyaspartate dehydratase activity. FEMS Microbiol Lett. 2003;225:189–193.10.1016/S0378-1097(03)00484-1
   PubMed Web of Science ®Google Scholar
• Murakami T, Maeda T, Yokota A, et al. Gene cloning and expression of pyridoxal 5′-phosphate-dependent L-threo-3-hydroxyaspartate dehydratase from Pseudomonas sp. T62, and characterization of the recombinant enzyme. J Biochem. 2009;145:661–668.10.1093/jb/mvp023
   PubMed Web of Science ®Google Scholar
• Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc Nat Acad Sci USA. 1988;85:2444–2448.10.1073/pnas.85.8.2444
   PubMed Web of Science ®Google Scholar
• Goto M, Yamauchi T, Kamiya N, et al. Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe. J Biol Chem. 2009;284:25944–25952.10.1074/jbc.M109.010470
   PubMed Web of Science ®Google Scholar
• Larkin MA, Blackshields G, Brown NP, et al. Clustal W and Clustal X version 2.0. Bioinformatics. 2007;23:2947–2948.10.1093/bioinformatics/btm404
   PubMed Web of Science ®Google Scholar
• Sigrist CJA, Cerutti L, de Castro E, et al. PROSITE, a protein domain database for functional characterization and annotation. Nucleic Acids Res. 2010;38:D161–D166.10.1093/nar/gkp885
   PubMed Web of Science ®Google Scholar
• Wada M, Matsumoto T, Nakamori S, et al. Purification and characterization of a novel enzyme, L-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62. FEMS Microbiol Lett. 1999;179:147–151.
   PubMed Web of Science ®Google Scholar
• Gibbs RG, Morris JG. Purification and properties of erythro-β-hydroxyaspartate dehydratase from Micrococcus denitrificans. Biochem J. 1965;97:547–554.10.1042/bj0970547
   PubMed Web of Science ®Google Scholar
• Ikegami T. Studies on the metabolism of β-hydroxyaspartic acid. Acta Med Okayama. 1975;29:241–247.
   PubMed Web of Science ®Google Scholar
• Kaletta C, Entian KD, Jung G. Prepeptide sequence of cinnamycin (Ro 09-0198): the first structural gene of a duramycin-type lantibiotic. Eur J Biochem. 1991;199:411–415.10.1111/ejb.1991.199.issue-2
   PubMedGoogle Scholar
• Scaloni A, Dalla Serra M, Amodeo P, et al. Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A. Biochem J. 2004;384:25–36.10.1042/BJ20040422
   PubMed Web of Science ®Google Scholar
• Ishiyama T, Furuta T, Takai M, et al. L-threo-β-hydroxyaspartic acid as an antibiotic amino acid. J Antibiot. 1975;28:821–823.10.7164/antibiotics.28.821
   PubMed Web of Science ®Google Scholar
• Wolosker H, Blackshaw S, Snyder SH. Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission. Proc Nat Acad Sci USA. 1999;96:13409–13414.10.1073/pnas.96.23.13409
   PubMed Web of Science ®Google Scholar
• De Miranda J, Santoro A, Engelender S, et al. Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene. 2000;256:183–188.10.1016/S0378-1119(00)00356-5
   PubMed Web of Science ®Google Scholar
• Katane M, Saitoh Y, Uchiyama K, et al. Characterization of a homologue of mammalian serine racemase from Caenorhabditis elegans: the enzyme is not critical for the metabolism of serine in vivo. Genes Cells. 2016;21:966–977.10.1111/gtc.2016.21.issue-9
   PubMed Web of Science ®Google Scholar
• Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annu Rev Biochem. 2004;73:383–415.10.1146/annurev.biochem.73.011303.074021
   PubMed Web of Science ®Google Scholar