Literature DB >> 12454494

Preliminary crystallographic studies of the creatinine amidohydrolase from Pseudomonas putida.

Kiyoshi Ito1, Naota Kanada, Takahiko Inoue, Kumiko Furukawa, Kinuyo Yamashita, Nobutada Tanaka, Kazuo T Nakamura, Yoshiaki Nishiya, Atsushi Sogabe, Tadashi Yoshimoto.   

Abstract

Creatinine amidohydrolase (creatininase; EC 3.5.2.10) from Pseudomonas putida has been overexpressed in Escherichia coli and crystallized by the hanging-drop method. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 102.0, b = 150.7, c = 167.1 A. Native data were collected to 1.8 A resolution by a rotation method at 100 K using an ADSC Quantum 4R CCD detector with synchrotron radiation.

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Year:  2002        PMID: 12454494     DOI: 10.1107/s0907444902017067

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Influence of metal cofactors and water on the catalytic mechanism of creatininase-creatinine in aqueous solution from molecular dynamics simulation and quantum study.

Authors:  Vannajan Sanghiran Lee; Kanchanok Kodchakorn; Jitrayut Jitonnom; Piyarat Nimmanpipug; Prachya Kongtawelert; Bhusana Premanode
Journal:  J Comput Aided Mol Des       Date:  2010-08-28       Impact factor: 3.686

  1 in total

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