Atrazine chlorohydrolase from Pseudomonas sp. strain ADP is a metalloenzyme.

Abstract:

:Atrazine chlorohydrolase (AtzA) from Pseudomonas sp. ADP initiates the metabolism of the herbicide atrazine by catalyzing a hydrolytic dechlorination reaction to produce hydroxyatrazine. Sequence analysis revealed AtzA to be homologous to metalloenzymes within the amidohydrolase protein superfamily. AtzA activity was experimentally shown to depend on an enzyme-bound, divalent transition-metal ion. Loss of activity obtained by incubating AtzA with the chelator 1,10-phenanthroline or oxalic acid was reversible upon addition of Fe(II), Mn(II), or Co(II) salts. Experimental evidence suggests a 1:1 metal to subunit stoichiometry, with the native metal being Fe(II). Our data show that the inhibitory effects of metals such as Zn(II) and Cu(II) are not the result of displacing the active site metal. Taken together, these data indicate that AtzA is a functional metalloenzyme, making this the first report, to our knowledge, of a metal-dependent dechlorinating enzyme that proceeds via a hydrolytic mechanism.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Seffernick JL,McTavish H,Osborne JP,de Souza ML,Sadowsky MJ,Wackett LP

doi

10.1021/bi020415s

subject

Has Abstract

pub_date

2002-12-03 00:00:00

pages

14430-7

issue

48

eissn

0006-2960

issn

1520-4995

pii

bi020415s

journal_volume

41

pub_type

杂志文章