Literature DB >> 8107120

Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.

C A Earhart1, M D Hall, I Michaud-Soret, L Que, D H Ohlendorf.   

Abstract

The metalloenzyme catechol 1,2-dioxygenase from Pseudomonas arvilla C-1 consists of three isozymes formed by combinations of two non-identical subunits; alpha alpha, alpha beta and beta beta; with molecular masses of 59,000, 63,000 and 67,000 Da, respectively. The alpha alpha isozyme crystallizes in the orthorhombic space group C222(1) with unit cell dimensions a = 62.7 A, b = 71.5 A, c = 187.1 A. The rectangular plates diffract to 2.6 A resolution. This is the first dioxygenase to be crystallized that uses catechol as a substrate. Comparison of the structure of this enzyme with protocatechuate 3,4-dioxygenase will provide basic information about the mechanisms of subunit association, substrate selectivity, and the origins of metabolic diversity in enzymes.

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Year:  1994        PMID: 8107120     DOI: 10.1006/jmbi.1994.1144

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  1 in total

1.  Chlorocatechols substituted at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase of Pseudomonas chlororaphis RW71.

Authors:  T Potrawfke; J Armengaud; R M Wittich
Journal:  J Bacteriol       Date:  2001-02       Impact factor: 3.490

  1 in total

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