Structure ofAcinetobacterStrain ADP1 Protocatechuate 3,4-Dioxygenase at 2.2 Å Resolution:  Implications for the Mechanism of an Intradiol Dioxygenase†

Biochemistry ◽  
2000 ◽  
Vol 39 (27) ◽  
pp. 7943-7955 ◽  
Author(s):  
Matthew W. Vetting ◽  
David A. D'Argenio ◽  
L. Nicholas Ornston ◽  
Douglas H. Ohlendorf
Keyword(s):  
Intradiol Dioxygenase

Characterization of the Maleylacetate Reductase MacA of Rhodococcus opacus 1CP and Evidence for the Presence of an Isofunctional Enzyme

1998 ◽  
Vol 180 (14) ◽  
pp. 3503-3508 ◽  
Author(s):  
Volker Seibert ◽  
Elena M. Kourbatova ◽  
Ludmila A. Golovleva ◽  
Michael Schlömann
Keyword(s):  
Aromatic Compounds ◽  
Gene Clusters ◽  
Reductive Dehalogenation ◽  
Rhodococcus Opacus ◽  
Reductase Gene ◽  
Rhodococcus Opacus 1Cp ◽  
Dienelactone Hydrolase ◽  
Maleylacetate Reductase ◽  
Intradiol Dioxygenase

ABSTRACT Maleylacetate reductases (EC 1.3.1.32 ) have been shown to contribute not only to the bacterial catabolism of some usual aromatic compounds like quinol or resorcinol but also to the degradation of aromatic compounds carrying unusual substituents, such as halogen atoms or nitro groups. Genes coding for maleylacetate reductases so far have been analyzed mainly in chloroaromatic compound-utilizing proteobacteria, in which they were found to belong to specialized gene clusters for the turnover of chlorocatechols or 5-chlorohydroxyquinol. We have now cloned the gene macA, which codes for one of apparently (at least) two maleylacetate reductases in the gram-positive, chlorophenol-degrading strain Rhodococcus opacus 1CP. Sequencing of macA showed the gene product to be relatively distantly related to its proteobacterial counterparts (ca. 42 to 44% identical positions). Nevertheless, like the known enzymes from proteobacteria, the cloned Rhodococcusmaleylacetate reductase was able to convert 2-chloromaleylacetate, an intermediate in the degradation of dichloroaromatic compounds, relatively fast and with reductive dehalogenation to maleylacetate. Among the genes ca. 3 kb up- and downstream of macA, none was found to code for an intradiol dioxygenase, a cycloisomerase, or a dienelactone hydrolase. Instead, the only gene which is likely to be cotranscribed with macA encodes a protein of the short-chain dehydrogenase/reductase family. Thus, the R. opacus maleylacetate reductase genemacA clearly is not part of a specialized chlorocatechol gene cluster.

scholarly journals Positive Selection for Mutations Affecting Bioconversion of Aromatic Compounds in Agrobacterium tumefaciens: Analysis of Spontaneous Mutations in the Protocatechuate 3,4-Dioxygenase Gene

2000 ◽  
Vol 182 (21) ◽  
pp. 6145-6153 ◽  
Author(s):  
Donna Parke
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Positive Selection ◽  
Aromatic Compounds ◽  
Spontaneous Mutation ◽  
Carbon Sources ◽  
Large Deletion ◽  
Missense Mutations ◽  
Amino Acid Residues ◽  
Selection For ◽  
Intradiol Dioxygenase

ABSTRACT A positive selection method for mutations affecting bioconversion of aromatic compounds was applied to a mutant strain ofAgrobacterium tumefaciens A348. The nucleotide sequence of the A348 pcaHGB genes, which encode protocatechuate 3,4-dioxygenase (PcaHG) and β-carboxy-cis,cis-muconate cycloisomerase (PcaB) for the first two steps in catabolism of the diphenolic protocatechuate, was determined. An omega element was introduced into the pcaB gene of A348, creating strain ADO2077. In the presence of phenolic compounds that can serve as carbon sources, growth of ADO2077 is inhibited due to accumulation of the tricarboxylate intermediate. The toxic effect, previously described forAcinetobacter sp., affords a powerful selection for suppressor mutations in genes required for upstream catabolic steps. By monitoring loss of the marker in pcaB, it was possible to determine that the formation of deletions was minimal compared to results obtained with Acinetobacter sp. Thus, the tricarboxylic acid trick in and of itself does not appear to select for large deletion mutations. The power of the selection was demonstrated by targeting the pcaHG genes of A. tumefaciensfor spontaneous mutation. Sixteen strains carrying putative second-site mutations in pcaH or -G were subjected to sequence analysis. All single-site events, their mutations revealed no particular bias toward multibase deletions or unusual patterns: five (−1) frameshifts, one (+1) frameshift, one tandem duplication of 88 bp, one deletion of 92 bp, one nonsense mutation, and seven missense mutations. PcaHG is considered to be the prototypical ferric intradiol dioxygenase. The missense mutations served to corroborate the significance of active site amino acid residues deduced from crystal structures of PcaHG from Pseudomonas putida andAcinetobacter sp. as well as of residues in other parts of the enzyme.

Characterization of an intradiol dioxygenase involved in the biodegradation of the chlorophenoxy herbicides 2,4-D and 2,4,5-T

FEBS Letters ◽  
1997 ◽  
Vol 407 (1) ◽  
pp. 69-72 ◽  
Author(s):  
V.M Travkin ◽  
A.P Jadan ◽  
F Briganti ◽  
A Scozzafava ◽  
L.A Golovleva
Keyword(s):  
Chlorophenoxy Herbicides ◽  
Intradiol Dioxygenase

scholarly journals Structure–Activity Relationships Delineate How the Maize Pathogen Cochliobolus heterostrophus Uses Aromatic Compounds as Signals and Metabolites

2012 ◽  
Vol 25 (7) ◽  
pp. 931-940 ◽  
Author(s):  
Samer Shalaby ◽  
Benjamin A. Horwitz ◽  
Olga Larkov
Keyword(s):  
Plant Pathogens ◽  
Inverse Correlation ◽  
Cochliobolus Heterostrophus ◽  
Strongly Correlated ◽  
Coumaric Acid ◽  
Nuclear Retention ◽  
Structure Activity ◽  
Wide Range ◽  
Dioxygenase Gene ◽  
Intradiol Dioxygenase

The necrotrophic maize pathogen Cochliobolus heterostrophus senses plant-derived phenolic compounds, which promote nuclear retention of the redox-sensitive transcription factor ChAP1 and alter gene expression. The intradiol dioxygenase gene CCHD1 is strongly upregulated by coumaric and caffeic acids. Plant phenolics are potential nutrients but some of them are damaging compounds that need to be detoxified. Using coumaric acid as an inducer (16 to 160 μM), we demonstrated the rapid and simultaneous upregulation of most of the β-ketoadipate pathway genes in C. heterostrophus. A cchd1 deletion mutant provided genetic evidence that protocatechuic acid is an intermediate in catabolism of a wide range of aromatic acids. Aromatics catabolism was slowed for compounds showing toxicity, and this was strongly correlated with nuclear retention of GFP-ChAP1. The activity of a structure series of compounds showed complementary requirements for upregulation of CCHD1 and for ChAP1 nuclear retention. Thus, there is an inverse correlation between the ability to metabolize a compound and the stress response (ChAP1 nuclear retention) that it causes. The ability to metabolize phenolics and to respond to them as signals should be an advantage to plant pathogens and may explain the presence of at least two response pathways detecting these compounds.

scholarly journals Elucidation of the 4-Hydroxyacetophenone Catabolic Pathway in Pseudomonas fluorescens ACB

2008 ◽  
Vol 190 (15) ◽  
pp. 5190-5198 ◽  
Author(s):  
Mariëlle J. H. Moonen ◽  
Nanne M. Kamerbeek ◽  
Adrie H. Westphal ◽  
Sjef A. Boeren ◽  
Dick B. Janssen ◽  
...  
Keyword(s):  
Pseudomonas Fluorescens ◽  
Efflux Pump ◽  
Intermediate Formation ◽  
Open Reading Frames ◽  
Ring Cleavage ◽  
Semialdehyde Dehydrogenase ◽  
Genes Encoding ◽  
Intradiol Dioxygenase ◽  
Extradiol Dioxygenases ◽  
Reading Frames

ABSTRACT The catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB is known to proceed through the intermediate formation of hydroquinone. Here, we provide evidence that hydroquinone is further degraded through 4-hydroxymuconic semialdehyde and maleylacetate to β-ketoadipate. The P. fluorescens ACB genes involved in 4-hydroxyacetophenone utilization were cloned and characterized. Sequence analysis of a 15-kb DNA fragment showed the presence of 14 open reading frames containing a gene cluster (hapCDEFGHIBA) of which at least four encoded enzymes are involved in 4-hydroxyacetophenone degradation: 4-hydroxyacetophenone monooxygenase (hapA), 4-hydroxyphenyl acetate hydrolase (hapB), 4-hydroxymuconic semialdehyde dehydrogenase (hapE), and maleylacetate reductase (hapF). In between hapF and hapB, three genes encoding a putative intradiol dioxygenase (hapG), a protein of the Yci1 family (hapH), and a [2Fe-2S] ferredoxin (hapI) were found. Downstream of the hap genes, five open reading frames are situated encoding three putative regulatory proteins (orf10, orf12, and orf13) and two proteins possibly involved in a membrane efflux pump (orf11 and orf14). Upstream of hapE, two genes (hapC and hapD) were present that showed weak similarity with several iron(II)-dependent extradiol dioxygenases. Based on these findings and additional biochemical evidence, it is proposed that the hapC and hapD gene products are involved in the ring cleavage of hydroquinone.

Vanadium catalyzed oxygenation of 4,6-di-tert-butylpyrogallol. A model reaction for intradiol dioxygenase

1983 ◽  
Vol 79 ◽  
pp. 104-105 ◽  
Author(s):  
Yoshitaka Tatsuno ◽  
Masanobu Tatsuda ◽  
Sei Otsuka ◽  
Kazuhide Tani
Keyword(s):  
Model Reaction ◽  
Intradiol Dioxygenase

scholarly journals Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad.

1975 ◽  
Vol 250 (13) ◽  
pp. 4848-4855
Author(s):  
M Fujiwara ◽  
L A Golovleva ◽  
Y Saeki ◽  
M Nozaki ◽  
O Hayaishi
Keyword(s):  
Intradiol Dioxygenase

The mechanism of the reaction of intradiol dioxygenase with hydroperoxy probe

2011 ◽  
Vol 169 (1) ◽  
pp. 207-216 ◽  
Author(s):  
Anna Wójcik ◽  
Tomasz Borowski ◽  
Ewa Broclawik
Keyword(s):  
Intradiol Dioxygenase ◽  
Mechanism Of The Reaction
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