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NTIS 바로가기FEBS letters, v.447 no.1, 1999년, pp.25 - 28
Ando, Susumu (National Institute of Bioscience and Human-Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan) , Ishikawa, Kazuhiko (National Institute of Bioscience and Human-Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan) , Ishida, Hiroyasu (National Institute of Bioscience and Human-Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan) , Kawarabayasi, Yutaka (National Institute of Bioscience and Human-Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan) , Kikuchi, Hisasi (National Institute of Technology and Evaluation, Nishihara, Shibuyaku, Tokyo 151-0066, Japan) , Kosugi, Yoshitsugu (National Institute of Bioscience and Human-Technology, 1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan)
AbstractFrom the genome sequence data of the thermophilic archaeon Pyrococcus horikoshii, an open reading frame was found which encodes a protein (332 amino acids) homologous with an endoglucanase from Clostridium thermocellum (42% identity), deblocking aminopeptidase from Pyrococcus furiosus (42% i...
González, Juan M., Masuchi, Yaeko, Robb, F. T., Ammerman, James W., Maeder, Dennis L., Yanagibayashi, Miki, Tamaoka, J., Kato, Chiaki. Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough. Extremophiles : life under extreme conditions, vol.2, no.2, 123-130.
Ishikawa, Kazuhiko, Ishida, Hiroyasu, Koyama, Yoshinori, Kawarabayasi, Yutaka, Kawahara, Jun-ichi, Matsui, Eriko, Matsui, Ikuo. Acylamino Acid-releasing Enzyme from the Thermophilic ArchaeonPyrococcus horikoshii. The Journal of biological chemistry, vol.273, no.28, 17726-17731.
Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J.-M., Moras, D., Tarnus, C.. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure, vol.2, no.4, 283-291.
Altschul, Stephen F., Gish, Warren, Miller, Webb, Meyers, Eugene W., Lipman, David J.. Basic Local Alignment Search Tool. Journal of molecular biology, vol.215, no.3, 403-410.
Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., Pease, L.R.. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, vol.77, no.1, 51-59.
Hiromi, Keitaro, Takasaki, Yoshiyuki, Ono, Sôzaburo. Kinetics of Hydrolytic Reaction Catalyzed by Crystalline Bacterial α-Amylase. III. The Influence of Temperature. Bulletin of the Chemical Society of Japan, vol.36, no.5, 563-569.
Doi, Etsushiro, Shibata, Daisuke, Matoba, Teruyoshi. Modified colorimetric ninhydrin methods for peptidase assay. Analytical biochemistry, vol.118, no.1, 173-184.
Kobayashi, K, Smith, J A. Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction.. The Journal of biological chemistry, vol.262, no.24, 11435-11445.
Gade, W., Brown, J.L.. Purification and partial characterization of alpha-N-acylpeptide hydrolase from bovine liver.. The Journal of biological chemistry, vol.253, no.14, 5012-5018.
Bailey, J.M., French, Dexter. THE SIGNIFICANCE OF MULTIPLE REACTIONS IN ENZYME-POLYMER SYSTEMS. The Journal of biological chemistry, vol.226, no.1, 1-14.
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