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Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formation.
Kato S, Mihara H, Kurihara T, Yoshimura T, Esaki N. Kato S, et al. Among authors: kurihara t. Biosci Biotechnol Biochem. 2000 Nov;64(11):2412-9. doi: 10.1271/bbb.64.2412. Biosci Biotechnol Biochem. 2000. PMID: 11193410
Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast, Candida tropicalis.
Kurihara T, Ueda M, Kanayama N, Kondo J, Teranishi Y, Tanaka A. Kurihara T, et al. Eur J Biochem. 1992 Dec 15;210(3):999-1005. doi: 10.1111/j.1432-1033.1992.tb17505.x. Eur J Biochem. 1992. PMID: 1362382
Physiological roles of acetoacetyl-CoA thiolase in n-alkane-utilizable yeast, Candida tropicalis: possible contribution to alkane degradation and sterol biosynthesis.
Kurihara T, Ueda M, Kamasawa N, Osumi M, Tanaka A. Kurihara T, et al. J Biochem. 1992 Dec;112(6):845-8. doi: 10.1093/oxfordjournals.jbchem.a123987. J Biochem. 1992. PMID: 1363552
The presence of two types of thiolases, acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase, was demonstrated in peroxisomes of n-alkane-grown Candida tropicalis [Kurihara, T., Ueda, M., & Tanaka, A. (1989) J. Biochem. 106, 474-478], while acetoacetyl-CoA thiol …
The presence of two types of thiolases, acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase, was demonstrated in peroxisomes of n-alkane-gr …
Beta-oxidation of butyrate, the short-chain-length fatty acid, occurs in peroxisomes in the yeast Candida tropicalis.
Kurihara T, Ueda M, Okada H, Kamasawa N, Naito N, Osumi M, Tanaka A. Kurihara T, et al. J Biochem. 1992 Jun;111(6):783-7. doi: 10.1093/oxfordjournals.jbchem.a123836. J Biochem. 1992. PMID: 1500419
Peroxisomal acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase from an n-alkane-utilizing yeast, Candida tropicalis: purification and characterization.
Kurihara T, Ueda M, Tanaka A. Kurihara T, et al. J Biochem. 1989 Sep;106(3):474-8. doi: 10.1093/oxfordjournals.jbchem.a122876. J Biochem. 1989. PMID: 2575092
Overexpression and feasible purification of thermostable L-2-halo acid dehalogenase of Pseudomonas sp. YL.
Liu JQ, Kurihara T, Nardi-Dei V, Okamura T, Esaki N, Soda K. Liu JQ, et al. Among authors: kurihara t. Biodegradation. 1995 Sep;6(3):223-7. doi: 10.1007/BF00700461. Biodegradation. 1995. PMID: 7579997
Unique primary structure of 2-nitropropane dioxygenase from Hansenula mrakii.
Tchorzewski M, Kurihara T, Esaki N, Soda K. Tchorzewski M, et al. Among authors: kurihara t. Eur J Biochem. 1994 Dec 15;226(3):841-6. doi: 10.1111/j.1432-1033.1994.00841.x. Eur J Biochem. 1994. PMID: 7813473
Comparative studies of genes encoding thermostable L-2-halo acid dehalogenase from Pseudomonas sp. strain YL, other dehalogenases, and two related hypothetical proteins from Escherichia coli.
Nardi-Dei V, Kurihara T, Okamura T, Liu JQ, Koshikawa H, Ozaki H, Terashima Y, Esaki N, Soda K. Nardi-Dei V, et al. Among authors: kurihara t. Appl Environ Microbiol. 1994 Sep;60(9):3375-80. doi: 10.1128/AEM.60.9.3375-3380.1994. Appl Environ Microbiol. 1994. PMID: 7944368 Free PMC article.
Purification and characterization of thermostable and nonthermostable 2-haloacid dehalogenases with different stereospecificities from Pseudomonas sp. strain YL.
Liu JQ, Kurihara T, Hasan AK, Nardi-Dei V, Koshikawa H, Esaki N, Soda K. Liu JQ, et al. Among authors: kurihara t. Appl Environ Microbiol. 1994 Jul;60(7):2389-93. doi: 10.1128/AEM.60.7.2389-2393.1994. Appl Environ Microbiol. 1994. PMID: 8074519 Free PMC article.
Crystallization and preliminary x-ray crystallographic studies of L-2-haloacid dehalogenase from Pseudomonas sp. YL.
Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K. Hisano T, et al. Among authors: kurihara t. Proteins. 1996 Apr;24(4):520-2. doi: 10.1002/(SICI)1097-0134(199604)24:4<520::AID-PROT12>3.0.CO;2-N. Proteins. 1996. PMID: 8860001
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