Kato DI - Search Results

1

Identification and characterization of substrate- and product-selective nylon hydrolases.

Drufva EE, Cahill JF, Saint-Vincent PMB, Williams AN, Bocharova V, Capra N, Meilleur F, Carper DL, Bourgery C, Miyazaki K, Yonemura M, Shiraishi Y, Parks JM, Zhou M, Dishner IT, Foster JC, Koehler SJ, Valentino HR, Sedova A, Kertesz V, Vasileva DP, Hochanadel LH, Figg CA, Negoro S, Kato DI, Chen SH, Michener JK. Drufva EE, et al. Among authors: kato di. bioRxiv [Preprint]. 2024 Nov 14:2024.11.14.623603. doi: 10.1101/2024.11.14.623603. bioRxiv. 2024. PMID: 39605696 Free PMC article. Preprint.

2

Structural and functional characterization of nylon hydrolases.

Negoro S, Kato DI, Ohki T, Yasuhira K, Kawashima Y, Nagai K, Takeo M, Shibata N, Kamiya K, Shigeta Y. Negoro S, et al. Among authors: kato di. Methods Enzymol. 2021;648:357-389. doi: 10.1016/bs.mie.2020.11.004. Epub 2020 Dec 29. Methods Enzymol. 2021. PMID: 33579412

3

X-ray crystallographic and mutational analysis of the NylC precursor: catalytic mechanism of autocleavage and substrate hydrolysis of nylon hydrolase.

Negoro S, Shibata N, Kato DI, Tanaka Y, Yasuhira K, Nagai K, Oshima S, Furuno Y, Yokoyama R, Miyazaki K, Takeo M, Hengphasatporn K, Shigeta Y, Lee YH, Higuchi Y. Negoro S, et al. Among authors: kato di. FEBS J. 2023 Jul;290(13):3400-3421. doi: 10.1111/febs.16755. Epub 2023 Mar 1. FEBS J. 2023. PMID: 36799721 Free article.

4

Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate.

Takehara I, Fujii T, Tanimoto Y, Kato DI, Takeo M, Negoro S. Takehara I, et al. Among authors: kato di. Appl Microbiol Biotechnol. 2018 Jan;102(2):801-814. doi: 10.1007/s00253-017-8657-y. Epub 2017 Nov 29. Appl Microbiol Biotechnol. 2018. PMID: 29188330

5

Nylon-oligomer degrading enzyme/substrate complex: catalytic mechanism of 6-aminohexanoate-dimer hydrolase.

Negoro S, Ohki T, Shibata N, Sasa K, Hayashi H, Nakano H, Yasuhira K, Kato D, Takeo M, Higuchi Y. Negoro S, et al. J Mol Biol. 2007 Jun 29;370(1):142-56. doi: 10.1016/j.jmb.2007.04.043. Epub 2007 Apr 24. J Mol Biol. 2007. PMID: 17512009

6

Draft Genome Sequence of the Nylon Oligomer-Degrading Bacterium Arthrobacter sp. Strain KI72.

Takehara I, Kato DI, Takeo M, Negoro S. Takehara I, et al. Among authors: kato di. Genome Announc. 2017 Apr 27;5(17):e00217-17. doi: 10.1128/genomeA.00217-17. Genome Announc. 2017. PMID: 28450506 Free PMC article.

7

Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a beta-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolase.

Ohki T, Shibata N, Higuchi Y, Kawashima Y, Takeo M, Kato D, Negoro S. Ohki T, et al. Protein Sci. 2009 Aug;18(8):1662-73. doi: 10.1002/pro.185. Protein Sci. 2009. PMID: 19521995 Free PMC article.

8

Identification and characterization of another 4-nitrophenol degradation gene cluster, nps, in Rhodococcus sp. strain PN1.

Yamamoto K, Nishimura M, Kato D, Takeo M, Negoro S. Yamamoto K, et al. J Biosci Bioeng. 2011 Jun;111(6):687-94. doi: 10.1016/j.jbiosc.2011.01.016. Epub 2011 Mar 10. J Biosci Bioeng. 2011. PMID: 21396889

9

Correction to: Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate.

Takehara I, Fujii T, Tanimoto Y, Kato DI, Takeo M, Negoro S. Takehara I, et al. Among authors: kato di. Appl Microbiol Biotechnol. 2018 Jan;102(2):815. doi: 10.1007/s00253-017-8682-x. Appl Microbiol Biotechnol. 2018. PMID: 29234852

10

Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase.

Negoro S, Shibata N, Lee YH, Takehara I, Kinugasa R, Nagai K, Tanaka Y, Kato DI, Takeo M, Goto Y, Higuchi Y. Negoro S, et al. Among authors: kato di. Sci Rep. 2018 Jun 27;8(1):9725. doi: 10.1038/s41598-018-27860-w. Sci Rep. 2018. PMID: 29950566 Free PMC article.

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