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Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli

Eichhorn, Eric, van der Ploeg, Jan R., Kertesz, Michael A., Leisinger, Thomas·1997·Journal of Biological Chemistry
DOI 10.1074/jbc.272.37.23031
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FIG. 1 Purification of the TauD protein from E. coli BL21(DE3)(pME4141). Protein samples were analyzed at different stages of the TauD purification on 10% SDS-polyacrylamide gels under reducing and denaturing conditions and stained with Coomassie Brilliant Blue. Lane M , molecular mass markers (indicated in kDa); lane A , uninduced cell extract (30 m g); lane B , extract of induced cells (30 m g); lane C , fraction precipitating between 50 and 60% ammonium sulfate (30 m g); lane D , purified TauD obtained after Resource Q chromatography (25 m g).
FIG. 1 Purification of the TauD protein from E. coli BL21(DE3)(pME4141). Protein samples were analyzed at different stages of the TauD purification on 10% SDS-polyacrylamide gels under reducing and denaturing conditions and stained with Coomassie Brilliant Blue. Lane M , molecular mass markers (indicated in kDa); lane A , uninduced cell extract (30 m g); lane B , extract of induced cells (30 m g); lane C , fraction precipitating between 50 and 60% ammonium sulfate (30 m g); lane D , purified TauD obtained after Resource Q chromatography (25 m g).CC-BY · From the PDF
FIG. 2 Overall reaction catalyzed by the a -KG-dependent taurine dioxygenase from E. coli .
FIG. 2 Overall reaction catalyzed by the a -KG-dependent taurine dioxygenase from E. coli .CC-BY · From the PDF
FIG. 3 Enzymatic reduction of the product of taurine desulfonation to ethanolamine. The formation of aminoacetaldehyde from taurine was followed by coupling the TauD-catalyzed reaction to horse liver alcohol dehydrogenase. The complete assay mixture contained (in a 1-ml volume) 1 mM taurine, 1 mM a -KG, 100 m M Fe(II)SO 4 , 200 m M ascorbate, 175 m M NADH, 3.2 units of alcohol dehydrogenase, and 500 milliunits of TauD. NADH consumption was monitored by measuring the absorbance at 340 nm. In the controls, NADH consumption was measured in reaction mixtures lacking TauD, alcohol dehydrogenase ( ADH ), taurine, or a -KG.
FIG. 3 Enzymatic reduction of the product of taurine desulfonation to ethanolamine. The formation of aminoacetaldehyde from taurine was followed by coupling the TauD-catalyzed reaction to horse liver alcohol dehydrogenase. The complete assay mixture contained (in a 1-ml volume) 1 mM taurine, 1 mM a -KG, 100 m M Fe(II)SO 4 , 200 m M ascorbate, 175 m M NADH, 3.2 units of alcohol dehydrogenase, and 500 milliunits of TauD. NADH consumption was monitored by measuring the absorbance at 340 nm. In the controls, NADH consumption was measured in reaction mixtures lacking TauD, alcohol dehydrogenase ( ADH ), taurine, or a -KG.CC-BY · From the PDF
FIG. 4 Kinetic constants of a -KG-dependent taurine dioxygenase. The effect of taurine and a -KG concentrations on initial rates was studied by keeping the concentration of one substrate at 600 m M while varying the concentration of the other substrate (25-500 m M taurine or 10-100 m M a -KG) in the standard assay mixture. Sulfite production was followed for 3 min by withdrawing samples every 15 or 30 s, and initial rates were calculated by regression analysis. A , effect of taurine concentration on the rate of desulfonation; B , effect of a -KG concentration on the rate of desulfonation.
FIG. 4 Kinetic constants of a -KG-dependent taurine dioxygenase. The effect of taurine and a -KG concentrations on initial rates was studied by keeping the concentration of one substrate at 600 m M while varying the concentration of the other substrate (25-500 m M taurine or 10-100 m M a -KG) in the standard assay mixture. Sulfite production was followed for 3 min by withdrawing samples every 15 or 30 s, and initial rates were calculated by regression analysis. A , effect of taurine concentration on the rate of desulfonation; B , effect of a -KG concentration on the rate of desulfonation.CC-BY · From the PDF
Image 5
CC-BY · From the PDF
FIG. 5 Alignment of amino acid sequences from TauD, TfdA, and related proteins. TauD is taurine dioxygenase from E. coli (Swissprot accession number P37610) (2). TfdA is 2,4-dichlorophenoxyacetate dioxygenase from A. eutrophus (Swissprot accession number P10088) (6). Y is a hypothetical protein of unknown function from M. tuberculosis (GenBank™ accession number Z77165; open reading frame MTCY78.22c), and Y 9 is a hypothetical protein of unknown function from S. cerevisiae (GenBank™ accession number Z47973; reverse complement translated from bases 13413 to 14650; only the sequence portion overlapping with the other three sequences is shown). Amino acid sequences were aligned using PILEUP (30). Conserved residues are boxed . Conserved His and Asp residues are marked with asterisks .
FIG. 5 Alignment of amino acid sequences from TauD, TfdA, and related proteins. TauD is taurine dioxygenase from E. coli (Swissprot accession number P37610) (2). TfdA is 2,4-dichlorophenoxyacetate dioxygenase from A. eutrophus (Swissprot accession number P10088) (6). Y is a hypothetical protein of unknown function from M. tuberculosis (GenBank™ accession number Z77165; open reading frame MTCY78.22c), and Y 9 is a hypothetical protein of unknown function from S. cerevisiae (GenBank™ accession number Z47973; reverse complement translated from bases 13413 to 14650; only the sequence portion overlapping with the other three sequences is shown). Amino acid sequences were aligned using PILEUP (30). Conserved residues are boxed . Conserved His and Asp residues are marked with asterisks .CC-BY · From the PDF

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Metadata

Authors
Eichhorn, E., van der Ploeg, J. R., Kertesz, M. A., & Leisinger, T.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-09
Volume
272
Issue
37
Pages
23031-23036
ISSN
0021-9258
DOI
10.1074/jbc.272.37.23031
Cited by
254
References
1
Language
en
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Eichhorn, E., van der Ploeg, J. R., Kertesz, M. A., & Leisinger, T. (1997). Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.272.37.23031