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Four Aromatic Intradiol Ring Cleavage Dioxygenases from Aspergillus niger.

Author(s): Semana P, Powlowski J

Ring cleavage dioxygenases catalyze the critical ring-opening step in the catabolism of aromatic compounds. The archetypal filamentous fungus Aspergillus niger previously has been reported to be able to utilize a range of monocyclic aromatic compounds as so...

Article GUID: 31540981
Characterization of active and inactive forms of the phenol hydroxylase stimulatory protein DmpM.

Author(s): Cadieux E, Powlowski J

Biochemistry. 1999 Aug 17;38(33):10714-22 Authors: Cadieux E, Powlowski J

Article GUID: 10451366
Biochemical and molecular characterization of a cellobiohydrolase from Trametes versicolor.

Author(s): Lahjouji K, Storms R, Xiao Z, Joung KB, Zheng Y, Powlowski J, Tsang A, Varin L

Appl Microbiol Biotechnol. 2007 May;75(2):337-46 Authors: Lahjouji K, Storms R, Xiao Z, Joung KB, Zheng Y, Powlowski J, Tsang A, Varin L

Article GUID: 17333176
A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compounds.

Author(s): Lei Y, Pawelek PD, Powlowski J

Biochemistry. 2008 Jul 01;47(26):6870-82 Authors: Lei Y, Pawelek PD, Powlowski J

Article GUID: 18537268
Analytical and computational approaches to define the Aspergillus niger secretome.

Author(s): Tsang A, Butler G, Powlowski J, Panisko EA, Baker SE

Fungal Genet Biol. 2009 Mar;46 Suppl 1:S153-S160 Authors: Tsang A, Butler G, Powlowski J, Panisko EA, Baker SE

Article GUID: 19618504
A molecular phylogeny of thermophilic fungi.

Author(s): Morgenstern I, Powlowski J, Ishmael N, Darmond C, Marqueteau S, Moisan MC, Quenneville G, Tsang A

Fungal Biol. 2012 Apr;116(4):489-502 Authors: Morgenstern I, Powlowski J, Ishmael N, Darmond C, Marqueteau S, Moisan MC, Quenneville G, Tsang A

Article GUID: 22483047
Transcriptome and exoproteome analysis of utilization of plant-derived biomass by Myceliophthora thermophila.

Author(s): Kolbusz MA, Di Falco M, Ishmael N, Marqueteau S, Moisan MC, Baptista CDS, Powlowski J, Tsang A

Fungal Genet Biol. 2014 Nov;72:10-20 Authors: Kolbusz MA, Di Falco M, Ishmael N, Marqueteau S, Moisan MC, Baptista CDS, Powlowski J, Tsang A

Article GUID: 24881579
mycoCLAP, the database for characterized lignocellulose-active proteins of fungal origin: resource and text mining curation support.

Author(s): Strasser K, McDonnell E, Nyaga C, Wu M, Wu S, Almeida H, Meurs MJ, Kosseim L, Powlowski J, Butler G, Tsang A

Database (Oxford). 2015;2015: Authors: Strasser K, McDonnell E, Nyaga C, Wu M, Wu S, Almeida H, Meurs MJ, Kosseim L, Powlowski J, Butler G, Tsang A

Article GUID: 25754864
Improvement in Saccharification Yield of Mixed Rumen Enzymes by Identification of Recalcitrant Cell Wall Constituents Using Enzyme Fingerprinting.

Author(s): Badhan A, Wang YX, Gruninger R, Patton D, Powlowski J, Tsang A, McAllister TA

Biomed Res Int. 2015;2015:562952 Authors: Badhan A, Wang YX, Gruninger R, Patton D, Powlowski J, Tsang A, McAllister TA

Article GUID: 26180803
Title:Characterization of active and inactive forms of the phenol hydroxylase stimulatory protein DmpM.
Authors:Cadieux E,  Powlowski J
Link:https://www.ncbi.nlm.nih.gov/pubmed/10451366?dopt=Abstract
DOI:10.1021/bi990835q
Category:Biochemistry
PMID:10451366
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada.

Description:

Characterization of active and inactive forms of the phenol hydroxylase stimulatory protein DmpM.

Biochemistry. 1999 Aug 17;38(33):10714-22

Authors: Cadieux E, Powlowski J

Abstract

The stimulatory protein DmpM of phenol hydroxylase from methylphenol-degrading Pseudomonas sp. strain CF600 has been found to exist in two forms. DmpM purified from the native strain was mostly active in stimulating phenol hydroxylase activity, whereas an inactive form accumulated in a recombinant strain. Both forms exhibited a molecular mass of 10 361.3 +/- 1.3 Da by electrospray mass spectrometry, but nondenaturing gel filtration showed molecular masses of 31 600 Da for the inactive form and 11 500 Da for the active form. Cross-linking and sedimentation velocity results were consistent with the inactive form being a dimer. Partial thermal or chemical denaturation, or treatment with trifluoroethanol, readily activated dimeric DmpM. A combination of circular dichroism and fluorescence spectroscopies, activity assays, and native and urea gel electrophoresis were used to further characterize reactivation with urea. These results showed that dissociation of the dimeric form of DmpM precedes denaturation at low protein concentrations and results in activation. The same concentration of urea that effects dissociation also converts the monomeric form to a different conformation.

PMID: 10451366 [PubMed - indexed for MEDLINE]