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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:A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compounds.
Authors:Lei Y,  Pawelek PD,  Powlowski J
Link:https://www.ncbi.nlm.nih.gov/pubmed/18537268?dopt=Abstract
DOI:10.1021/bi800349k
Category:Biochemistry
PMID:18537268
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Concordia University, 7141 Sherbrooke Street West, Montreal, Quebec, Canada.

Description:

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

Biochemistry. 2008 Jul 01;47(26):6870-82

Authors: Lei Y, Pawelek PD, Powlowski J

Abstract

The meta-cleavage pathway for catechol is a central pathway for the bacterial dissimilation of a wide variety of aromatic compounds, including phenols, methylphenols, naphthalenes, and biphenyls. The last enzyme of the pathway is a bifunctional aldolase/dehydrogenase that converts 4-hydroxy-2-ketovalerate to pyruvate and acetyl-CoA via acetaldehyde. The structure of the NAD (+)/CoASH-dependent aldehyde dehydrogenase subunit is similar to that of glyceraldehyde-3-phosphate dehydrogenase, with a Rossmann fold-based NAD (+) binding site observed in the NAD (+)-enzyme complex [Manjasetty, B. A., et al. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 6992-6997]. However, the location of the CoASH binding site was not determined. In this study, hydrogen-deuterium exchange experiments, coupled with peptic digest and mass spectrometry, were used to examine cofactor binding. The pattern of hydrogen-deuterium exchange in the presence of CoASH was almost identical to that observed with NAD (+), consistent with the two cofactors sharing a binding site. This is further supported by the observations that either CoASH or NAD (+) is able to elute the enzyme from an NAD (+) affinity column and that preincubation of the enzyme with NAD (+) protects against inactivation by CoASH. Consistent with these data, models of the CoASH complex generated using AUTODOCK showed that the docked conformation of CoASH can fully occupy the cavity containing the enzyme active site, superimposing with the NAD (+) cofactor observed in the X-ray crystal structure. Although CoASH binding Rossmann folds have been described previously, this is the first reported example of a Rossmann fold that can alternately bind CoASH or NAD (+) cofactors required for enzymatic catalysis.

PMID: 18537268 [PubMed - indexed for MEDLINE]