PAPERS
2023
Watabe, Y., Takahashi, S. (2023) Production of enhanced carotenoid-producing strains of the yeast Rhodottorula gracilis using the antibiotic Zeocine. Appl Biochem Biotech, In press.
Imanishi, D., Takahashi, S. (2023) RNA sequencing data analysis of the yeast Vanrija (Cryptococcus) humicola strain UJ1 grown on L- and D-aspartate. Data in brief, 47:109008. doi: 10.1016/j.dib.2023.109008..
2022
Kajitani K, Ishikawa T, Kobayashi T, Asato M, Shibata K, Kouya T, Takahashi S. (2022) DOI: 10.1007/s00253-022-11870-w. Appl Microbiol Biotechnol, 106(7), 2651-2663. https://doi.org/10.1007/s00253-022-11870-w.
2021
Imanishi, D.; Zaitsu, S.; Takahashi, S. Regulation of D-Aspartate Oxidase Gene Expression by Pyruvate Metabolism in the Yeast Cryptococcus humicola. Microorganisms 2021, 9, 2444. https://www.mdpi.com/2076-2607/9/12/2444
Kajitani K and Takahashi S. (2021) Complete genome sequence of Latilactobacillus sp. strain WDN19, a high-D-aspartate-producing lactic acid bacterium isolated from a Japanese pickle. Microbiol Resour Announc, 10(34), https://doi.org/10.1128/MRA.00568-21.
Kajitani K, Ishikawa T, Shibata K, Kouya T, Kera Y, Takahashi S. (2021) Development of an enzymatic screening method for D-aspartate-producing lactic acid bacteria. Enzyme Microbial Tech, 149, 109835. https://doi.org/10.1016/j.enzmictec.2021.109835
Imanishi D, Kera Y, Takahashi S. (2021) Identification of an acidic amino acid permease involved in D-aspartate uptake in the yeast Cryptococcus humicola. Microorganisms, 9(1), 192. https://doi.org/10.3390/microorganisms9010192
2020
Shimekake Y, Hirato Y, Funabashi R, Okazaki S, Goto M, Furuichi T, Suzuki H, Kera Y, Takahashi S. (2020) X-ray structure analysis of a unique D-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA. Acta Crystallogr. F Struct. Biol. Commun. 76(11), 517-523. https://doi.org/10.1107/S2053230X20013333
Shibata K, Imanishi D, Abe K, Suzuki M, Takahashi S, Kera Y. (2020) D-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-D-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice. BBA - PROTEINS PROTEOM. https://doi.org/10.1016/j.bbapap.2020.140527
Takahashi S. (2020) D-Aspartate oxidase: distribution, functions, properties, and biotechnological applications. Appl. Microbiol. Biotechnol., 104: 2883-2895. https://doi.org/10.1007/s00253-020-10439-9
Takahashi S, Morooka Y, Kumakura T, Abe K, Kera Y. (2020) Enzymatic characterization and regulation of gene expression of PhoK alkaline phosphatase in Sphingobium sp. strain TCM1. Appl. Microbiol. Biotechnol., 104, 1125-1134. https://doi.org/10.1007/s00253-019-10291-6
2019
Shibata K, Sugaya N, Kuboki Y, Matsuda H, Abe K, Takahashi S, Kera Y. Aspartate racemase and D-aspartate in starfish; possible involvement in testicular maturation. Biosci. Biotech. Biochem., https://doi.org/10.1080/09168451.2019.1660614.
Shimekake Y, Furuichi T, Abe K, Kera Y, Takahashi S. A novel thermostable D-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA. Sci. Rep., 2019, 9: 11948. https://www.nature.com/articles/s41598-019-48480-y.
Takahashi S, Osugi K, Shimekake Y, Shinbo A, Abe K, Kera Y. Characterization and improvement of substrate-binding affinity of D-aspartate oxidase of the thermophilic fungus Thermomyces dupontii. Appl. Microbiol. Biotechnol., 103(10), 4053-4064, 2019. https://doi.org/10.1007/s00253-019-09787-y
2018
Imanishi, D., Abe, K., Kera, Y., Takahashi, S. Draft genome sequence of the yeast Vanrija humicola (Formerly Cryptococcus humicola) strain UJ1, a producer of D-aspartate oxidase. Genome Announc. https://doi.org/10.1128/genomeA.00068-18
2017
Takahashi S, Abe K, Shibata K, Kera Y. (2017) Functions and metabolism of D-amino acids in microorganisms. In: The handbook of microbial metabolism of amino acids (D'Mello, J.P.F., Editor)., CAB International, Wallingford, UK, pp.315-331. DOI: 10.1079/9781780647234.0315.
Mizobuchi, T., Nonaka, R., Yoshimura, M., Abe, K., Takahashi, S., Kera, Y., Goto, M. (2017) Crystal structure of a pyridoxal 5′-phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca broughtonii. Acta Cryst., F73, 651-656.
Abe,K., Mukai, N., Morooka, Y., Makino, T., Oshima, K., Takahashi, S., Kera, Y. (2017) An atypical phosphodiesterase capable of degrading haloalkyl phosphate diesters from Sphingobium sp. strain TCM1. Sci. Rep., 7, 2842.
2016
Takayama, K., Sakamoto, C., Takahashi, S., Abe, K., Hirobe, A., Koshigiri, T. (2016) Construction of a D-valine sensor using D-amino acid oxidase of Rubrobacter xylanophilus. J. Technology and Education, 23, 57-61
Takahashi, S., Katanuma, H., Abe, K., Kera, Y. (2016) Identification of alkaline phosphatase genes for utilizing a flame retardant, tris(2-chloroethyl) phosphate, in Sphingobium sp. strain TCM1. Appl. Microbiol. Biotechnol.,101, 2153-2162
Kera, Y., Abe, K., Kasai, D., Fukuda, M., Takahashi, S. (2016) Draft genome sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp. strain TDK1, haloalkyl phosphate flame retardant and plasticizer-degrading bacteria. Genome Announc.,4, e00668-16
Takahashi, S., Shimada, K., Nozawa, S., Goto, M., Abe, K., Kera, Y. (2016) Possible role of a histidine residue in the substrate specificity of yeast D-aspartate oxidase. J. Biochem.,159, 371-378
Before 2015
Takahashi S, Abe K, Kera Y. (2015) Bacterial D-amino acid oxidases: Recent findings and future perspectives. Bioengineered, 6(4): 237-241. https://doi.org/10.1080/21655979.2015.1052917.
Takahashi, S., Furukawara, M., Omae, K., Tadokoro, N., Saito, Y., Abe, K. and Kera, Y. (2014) A highly stable D-amino acid oxidase of the thermophilic bacterium Rubrobacter xylanophilus. Appl. Environ. Microbiol., 80, 7219-7229
Takahashi, S., Okada, H., Abe, K. and Kera, Y. (2014) Genetic transformation of the yeast Rhodotorula gracilis ATCC 26217 by electroporation. Appl. Biochem. Microbiol., 50, 624-628
Abe, K., Yoshida, Y., Suzuki, Y., Mori, J., Doi, Y., Takahashi, S. and Kera, Y. (2014) Haloalkylphosphorus hydrolases purified from Sphingomonas sp. strain TDK1 and Sphingobium sp. strain TCM1. Appl. Environ. Microbiol., 80, 5866-5873
Saito, Y., Takahashi, S., Kobayashi, M., Abe, K. and Kera, Y. (2014) D-Amino acid oxidase of Streptomyces coelicolor and the effect of D-amino acids on the bacterium. Annal. Microbiol., 64, 1167-1177
Takahashi, S., Okada, H., Abe, K. and Kera, Y. (2012) D-amino acid-induced expression of D-amino acid oxidase in the yeast Schizosaccharomyces pombe. Curr. Microbiol., 65, 764-769
Kato, S., Ikuta, T., Hemmi, H., Takahashi, S., Kera, Y. and Yoshimura, T. (2012) Enzymatic assay for D-aspartic acid using D-aspartate oxidase and oxaloacetate decarboxylase. Biosci. Biotechnol. Biochem., 76, 2150-2152
Takahashi, S., Miura, K., Abe, K. and Kera, Y. (2012) Complete detoxification of tris(2-chloroethyl) phosphate by two bacterial strains: Sphingobium sp. strain TCM1 and Xanthobacter autotrophicus strain GJ10. J. Biosci. Bioeng., 114, 306-311
Takahashi, S., Obana, Y., Okada, S., Abe, K. and Kera, Y. (2012) Complete detoxification of tris(1,3-dichloro-2-propyl) phosphate by mixed two bacteria, Sphingobium sp. strain TCM1 and Arthrobacter sp. strain PY1. J. Biosci. Bioeng., 113, 79-83.
Shibata K., Sugaya N., Ono W., Abe K., Takahashi S. and Kera Y. (2011) Determination of D-aspartate N-methyltransferase activity in the starfish by direct analysis of N-methyl-D-aspartate with high-performance liquid chromatography. J. Chromatogr. B, 879, 3229-3234.
Takahashi S., Nakajima Y., Imaizumi T., Furuta Y., Ohshiro Y., Abe K., Yamada R. and Kera Y. (2011) Development of an autonomously replicating linear vector of the yeast Cryptococcus humicola by using telomere-like sequence repeats. Appl. Microbiol. Biotechnol., 89, 1213-1221.
Takahashi, S., Satake, I., Konuma, I., Kawashima, K., Kawasaki, M., Mori, S., Morino, J., Mori, J., Xu, H., Abe, K., Yamada, R. and Kera, Y. (2010) Isolation and identification of persistent chlorinated organophosphorus flame retardants-degrading bacteria., Appl. Environ. Microbiol., 76, 5292-5296.
Takahashi, S., Matsumoto, S., Maruyama, K., Wakaizumi, A., Abe, K., Kera,Y. and Yamada, R. (2009) An active-site mutation enhances the catalytic activity of the yeast Cryptococcus humicola D-aspartate oxidase. J. Mol. Catal. B: Enzymatic,61, 235-240.
Sato, R., Matsumoto, T., Hidaka, N., Imai, Y., Abe, K., Takahashi, S., Yamada, R. and Kera,Y. (2009) Cloning and expression of carp acetylcholinesterase gene in Pichia pastoris and characterization of the recombinant enzyme. Protein Expr. Purif., 64, 205-212.
Takahashi, S., Kawashima, K., Kawasaki, M., Kamito, J., Endo, Y., Akatsu, K., Horino, S., Yamada, R. and Kera, Y. (2008) Enrichment and characterization of chlorinated oganophosphate esters-degrading mixed bacterial cultures. J. Biosci. Bioeng., 106, 27-32.
Sato, R., Mitani, K., Matsumoto, T., Takahashi, S., Yamada, R. and Kera, Y. (2007) Effects of insecticides in vitro on acetylcholinesterase purified from body muscle of Koi carp (Cyprinus carpio). Jpn. J. Environ. Toxicol., 10, 31-38.
Abe, K., Takahashi, S., Muroki, Y., Kera, Y. and Yamada, R. (2006) Cloning and expression of the pyridoxal 5'-phosphate-dependent aspartate racemase gene from the bivalve mollusk Scapharca broughtonii and characterization of the recombinant enzyme. J. Biochem., 139, 235-244.
Takahashi, S., Kakuichi, T., Fujii, K., Kera, Y. and Yamada, R. (2005) Physiological role of D-aspartate oxidase in the assimilation and detoxification of D-aspartate in the yeast Cryptococcus humicola. Yeast, 22, 1203-1212.
Watanabe, T., Shibata, K., Kera, Y., Takahashi, S. and Yamada, R. (2005) Effects of hypoxic and osmottic stress on the free D-aspartate level in the muscle of blood shell Scapharca broughtonii. Amino Acids, 28, 291-296.
Oshima, K., Nakajima, H., Takahashi, S., Kera, Y., Shimomura, M. and Miyauchi, S. (2005) Quartz crystal microbalance assay for determination of plasma vitellogenin. Sensors and Actuators B, 105, 473-478.
Kera, Y., Mitani, K., Matsumoto, T., Sato, R., Takahashi, S. and Yamada, R. (2004) Acetylcholinesterase from Koi carp body muscle: tissue distribution, purification and characterization. Jpn. J. Environ. Toxicol., 7, 35-47.
Takahashi, S., Takahashi, T., Kera, R., Matsunaga, R., Shibuya, H. and Yamada, R. (2004) Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. J. Biochem., 135, 533-540.
Takahashi, S., Matsunaga, R., Kera, Y. and Yamada, R. (2003) Isolation of the Cryptococcus humicolus URA3 gene encoding orotidine-5'-phosphate decarboxylase and its use as a selective marker for transformation. J. Biosci. Bioeng., 96, 23-31.
Shibata, K., Watanabe, T., Yoshikawa, H., Abe K., Takahashi, S., Kera, Y. and Yamada, R. (2003) Nucleotides modulate the activity of aspartate racemase of Scapharca broughtonii. Comp. Biochem. Physiol. Part B, 134, 713-719.
Shibata, K., Watanabe, T., Yoshikawa, H., Abe, K., Takahashi, S., Kera, Y. and Yamada, R. (2003) Purification and characterization of aspartate racemase from the bivalve mollusk Scapharca broughtonii. Comp. Biochem. Physiol. Part B, 134, 307-314.
Tarui, A., Shibata, K., Takahashi, S., Kera, Y., Munegumi, T. and Yamada, R. (2003) N-Methyl-D-glutamate and N-methyl-L-glutamate in Scapharca broughtonii (Mollusca) and other invertebrates. Comp. Biochem. Physiol. Part B, 134, 79-87.
Kera, Y.,Koshiba, K., Hayakawa, S., Kato, T., Tsukada, Y., Ishikawa, H., Itoh, Y., Ibaraki, T., Kawata, K., Takahashi, S. and Yamada, R. (2002) Plasma vitellogenin concentration of juvenile Koi carp (Cyprinus carpio) exposed in situ to effluent from a sewage treatment works. Jpn. J. Environ. Toxicol., 5, 75-89.
Shibata, K., Tarui, A., Todoroki, N., Kawamoto, S., Takahashi, S., Kera, Y. and Yamada, R. (2001) Occurrence of N-methyl-L-aspartate in bivalves and its distribution compared with that of N-methy-D-aspartate and D,L-aspartate. Comp. Biochem. Physiol. Part B, 130, 493-500.
Kera, Y., Koshiba, K., Kato, T., Hayakawa, S., Takahashi, S., and Yamada, R. (2001) Plasma vitellogenin concentration of wild Koi carp (Cyprinus carpio) in the Shinano River and wetland sites in Niigata Prefecture. Jpn. J. Environ. Toxicol., 4, 35-43.