Crystal structure of catalase HPII from Escherichia coli (Q27729861)

ChEBI release 2020-05-28

N Verdaguer

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Jerónimo Bravo

object named as

J Bravo

1

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author name string

J Tormo

3

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C Betzel

4

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J Switala

5

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P C Loewen

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I Fita

Three-dimensional structure of the enzyme catalase

7

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publication date

15 May 1995

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published in

Structure

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volume

3

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issue

5

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page(s)

491-502

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cites work

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Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution

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Structure of beef liver catalase

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Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH.

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Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product

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The NADPH binding site on beef liver catalase

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The active center of catalase

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Molecular evolutionary analysis based on the amino acid sequence of catalase

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Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d.

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Probing Structure-Function Relations in Heme-Containing Oxygenases and Peroxidases

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

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Cloning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli.

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Crystallization and preliminary X-ray diffraction analysis of catalase HPII from Escherichia coli

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The locked rotation function

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Structure of a human common cold virus and functional relationship to other picornaviruses

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