CoChat
Sign Up
Cited by 254

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

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
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.272.37.23031

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

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

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Research works printed but not linked: 25

  1. Uria-Nickelsen, 1993, J. Gen. Microbiol., 139, 203, 10.1099/00221287-139-2-203 · DOI
  2. van der Ploeg, 1996, J. Bacteriol., 178, 5438, 10.1128/jb.178.18.5438-5446.1996 · DOI
  3. Uria-Nickelsen, 1994, Arch. Microbiol., 161, 434, 10.1007/BF00288955 · DOI
  4. Fukumori, 1993, J. Bacteriol., 175, 2083, 10.1128/jb.175.7.2083-2086.1993 · DOI
  5. Fukumori, 1993, J. Biol. Chem., 268, 24311, 10.1016/S0021-9258(20)80527-4 · DOI
  6. Studier, 1990, Methods Enzymol., 185, 60, 10.1016/0076-6879(90)85008-C · DOI
  7. Casadaban, 1976, J. Mol. Biol., 104, 541, 10.1016/0022-2836(76)90119-4 · DOI
  8. O'Neill, 1991, J. Bacteriol., 173, 94, 10.1128/jb.173.1.94-100.1991 · DOI
  9. Yanisch-Perron, 1985, Gene ( Amst. ), 33, 103, 10.1016/0378-1119(85)90120-9 · DOI
  10. Johnston, 1975, Antonie Leeuwenhoek, 41, 493, 10.1007/BF02565092 · DOI
  11. Riddles, 1983, Methods Enzymol., 91, 49, 10.1016/S0076-6879(83)91010-8 · DOI
  12. Bradford, 1976, Anal. Biochem., 72, 248, 10.1016/0003-2697(76)90527-3 · DOI · Paper page
  13. Prescott, 1993, J. Exp. Bot., 44, 849, 10.1093/jxb/44.5.849 · DOI
  14. Stoll, 1990, Methods Enzymol., 182, 24, 10.1016/0076-6879(90)82006-N · DOI
  15. Thysse, 1974, Antonie Leeuwenhoek, 40, 25, 10.1007/BF00394550 · DOI
  16. Higgins, 1996, Microbiology, 142, 251, 10.1099/13500872-142-2-251 · DOI
  17. Majamaa, 1984, Eur. J. Biochem., 138, 239, 10.1111/j.1432-1033.1984.tb07907.x · DOI
  18. Ng, 1991, J. Biol. Chem., 266, 1526, 10.1016/S0021-9258(18)52326-7 · DOI
  19. Puistola, 1980, Biochim. Biophys. Acta, 611, 40, 10.1016/0005-2744(80)90040-6 · DOI
  20. Don, 1985, J. Bacteriol., 161, 85, 10.1128/jb.161.1.85-90.1985 · DOI
  21. Myllyharju, 1997, EMBO J., 16, 1173, 10.1093/emboj/16.6.1173 · DOI
  22. Pirskanen, 1996, J. Biol. Chem., 271, 9398, 10.1074/jbc.271.16.9398 · DOI
  23. Borovok, 1996, Biochemistry, 35, 1981, 10.1021/bi951534t · DOI
  24. Roach, 1995, Nature, 375, 700, 10.1038/375700a0 · DOI
  25. Whiting, 1997, J. Am. Chem. Soc., 119, 3413, 10.1021/ja964449x · DOI

Cited by

Sorted by citations

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
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review