Substrate‐specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum: Biochemical and molecular analysis

Wagner, Matthias; Sonntag, Denise; Grimm, Rudolf; Pich, Andreas; Eckerskorn, Christoph; Söhling, Brigitte; Andreesen, Jan R.

doi:10.1046/j.1432-1327.1999.00107.x

Cited by 74Selenium in Biological SystemsOrganoselenium and organotellurium chemistryRedox biology and oxidative stress

Substrate‐specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum: Biochemical and molecular analysis

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Wagner, Matthias, Sonntag, Denise, Grimm, Rudolf, Pich, Andreas, Eckerskorn, Christoph, Söhling, Brigitte, Andreesen, Jan R.·1999·European Journal of Biochemistry

DOI 10.1046/j.1432-1327.1999.00107.x

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Abstract

The substrate‐specific selenoprotein B of glycine reductase (PB glycine) from Eubacterium acidaminophilum was purified and characterized. The enzyme consisted of three different subunits with molecular masses of about 22 (α), 25 (β) and 47 kDa (γ), probably in an α 2 β 2 γ 2 composition. PB glycine purified from cells grown in the presence of [75 Se]selenite was labeled in the 47‐kDa subunit. The 22‐kDa and 47‐kDa subunits both reacted with fluorescein thiosemicarbazide, indicating the presence of a carbonyl compound. This carbonyl residue prevented N‐terminal sequencing of the 22‐kDa (α) subunit, but it could be removed for Edman degradation by incubation with o‐phenylenediamine. A DNA fragment was isolated and sequenced which encoded β and α subunits of PB glycine (grdE), followed by a gene encoding selenoprotein A (grdA2) and the γ subunit of PB glycine (grdB2). The cloned DNA fragment represented a second GrdB‐encoding gene slightly different from a previously identified partial grdB1‐containing fragment. Both grdB genes contained an in‐frame UGA codon which confirmed the observed selenium content of the 47‐kDa (γ) subunit. Peptide sequence analyses suggest that grdE encodes a proprotein which is cleaved into the previously sequenced N‐terminal 25‐kDa (β) subunit and a 22‐kDa (α) subunit of PB glycine. Cleavage most probably occurred at an ‐Asn‐Cys‐ site concomitantly with the generation of the blocking carbonyl moiety from cysteine at the α subunit.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684 · see citing works
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572 · see citing works
A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids.
Wessel, D., & Flügge, U. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90782-6 · Cited by 3,997 · see citing works
Preparation of transforming deoxyribonucleic acid by phenol treatment
Saito, H., & Miura, K. (1963) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects · doi:10.1016/0926-6550(63)90386-4 · Cited by 1,814 · see citing works
A SPECIFIC MICROMETHOD FOR THE DETERMINATION OF ACYL PHOSPHATES
Lipmann, F. A., & Lc, T. (1945) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51298-4 · Cited by 1,422 · see citing works
Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197 · see citing works
SELENOCYSTEINE
Stadtman, T. C. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.000503 · Cited by 827 · see citing works
Comprehensive biological catalysis
Dafforn, T. R., & CLARKE, A. B. (1998) · Academic Press eBooks · Cited by 649 · see citing works
Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli.
Zinoni, F., Birkmann, A., Stadtman, T. C., & Böck, A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4650 · Cited by 486 · see citing works
Knowing when not to stop: selenocysteine incorporation in eukaryotes
Low, S. C., & Berry, M. J. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)80016-8 · Cited by 435 · see citing works
Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons.
Berry, M. J., Banu, L., Harney, J. W., & Larsen, P. R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06001.x · Cited by 428 · see citing works
The identity of the base following the stop codon determines the efficiency of in vivo translational termination in Escherichia coli.
Poole, E. S., Brown, C. M., & Tate, W. P. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb06985.x · Cited by 267 · see citing works
PYRUVOYL-DEPENDENT ENZYMES
van Poelje, P. D., & Snell, E. E. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.000333 · Cited by 243 · see citing works
Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium.
Axley, M. J., Böck, A., & Stadtman, T. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.19.8450 · Cited by 231 · see citing works
Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein
Turner, D. C., & Stadtman, T. C. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90069-6 · Cited by 220 · see citing works
The Formation of Diselenide Bridges in Proteins by Incorporation of Selenocysteine Residues: Biosynthesis and Characterization of (Se)2-Thioredoxin
Mueller, S., Senn, H., Gsell, B., Vetter, W., Baron, C., & Boeck, A. (1994) · Biochemistry · doi:10.1021/bi00177a034 · Cited by 175 · see citing works
Eubacterium acidaminophilum sp. nov., a versatile amino acid-degrading anaerobe producing or utilizing H2 or formate
Zindel, U., Freudenberg, W., Rieth, M., Andreesen, J. R., Schnell, J., & Widdel, F. (1988) · Archives of Microbiology · doi:10.1007/bf00407789 · Cited by 168 · see citing works
Self-citation
RNA Structure and Function
Liu, D. (2024) · CRC Press eBooks · doi:10.1201/9781003055211-13 · Cited by 157 · see citing works
Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion
Wilting, R., Schorling, S., Persson, B. C., & Böck, A. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0812 · Cited by 150 · see citing works
Glycine metabolism in anaerobes
Andreesen, J. R. (1994) · Antonie van Leeuwenhoek · doi:10.1007/bf00871641 · Cited by 116 · see citing works
Self-citation
Domain Structure of the Prokaryotic Selenocysteine-specific Elongation Factor SelB
Kromayer, M., Wilting, R., Tormay, P., & Böck, A. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0525 · Cited by 114 · see citing works
Diversity of Bacterial Respiratory Systems
Kowles, C. J. (2018) · CRC Press eBooks · doi:10.1201/9781351071499 · Cited by 106 · see citing works
The nature of the minimal 'selenocysteine insertion sequence' (SECIS) in Escherichia coli
Liu, Z. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.4.896 · Cited by 103 · see citing works
Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.
Baron, C., Heider, J., & Böck, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4181 · Cited by 100 · see citing works
[33] Specific modification of NH2-terminal residues by transamination
Dixon, H. B. F., & Fields, R. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(72)25036-4 · Cited by 84 · see citing works
Reductive cleavage of sarcosine and betaine by Eubacterium acidaminophilum via enzyme systems different from glycine reductase
Hormann, K., & Andreesen, J. R. (1989) · Archives of Microbiology · doi:10.1007/bf00277541 · Cited by 83 · see citing works
Self-citation
Solution structure of mRNA hairpins promoting selenocysteine incorporation in Escherichia coli and their base-specific interaction with special elongation factor SELB.
Hüttenhofer, A., Westhof, E., & Böck, A. (1996) · PubMed · Cited by 78 · see citing works
In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB
Klug, S. J., Hüttenhofer, A., Kromayer, M., & Famulok, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6676 · Cited by 77 · see citing works
Clostridial glycine reductase complex. Purification and characterization of the selenoprotein component.
Cone, J. E., del Rı́o, R. M., & Stadtman, T. C. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63352-1 · Cited by 68 · see citing works
The molecular basis of bacterial metabolism
(1991) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(91)90354-f · Cited by 61 · see citing works
Selenium-dependent clostridial glycine reductase. Purification and characterization of the two membrane-associated protein components.
Tanaka, H., & Stadtman, T. C. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37938-3 · Cited by 60 · see citing works
Clostridium halophilium sp. nov. and C. litorale sp. nov., an obligate halophilic and a marine species degrading betaine in the Stickland reaction
Fendrich, C., Hippe, H., & Gottschalk, G. (1990) · Archives of Microbiology · doi:10.1007/bf00423321 · Cited by 58 · see citing works
Selenocysteine Inserting RNA Elements Modulate GTP Hydrolysis of Elongation Factor SelB
Hüttenhofer, A., & Böck, A. (1998) · Biochemistry · doi:10.1021/bi972298k · Cited by 53 · see citing works
The Selenocysteine-Inserting tRNA Species: Structure and Function
Baron, C., & Böck, A. (2014) · ASM Press eBooks · doi:10.1128/9781555818333.ch26 · Cited by 52 · see citing works
Purification and Characterization of Protein PB of Betaine Reductase and its Relationship to the Corresponding Proteins Glycine Reductase and Sarcosine Reductase from Eubacterium Acidaminophilum
Meyer, M., Granderath, K., & Andreesen, J. R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.184_c.x · Cited by 51 · see citing works
Self-citation
Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB.Preprint
Ringquist, S., Schneider, D., Gibson, T. J., Baron, C., Böck, A., & Gold, L. (1994) · Genes & Development · doi:10.1101/gad.8.3.376 · Cited by 48 · see citing works
Selenoprotein A component of the glycine reductase complex from Clostridium purinolyticum: nucleotide sequence of the gene shows that selenocysteine is encoded by UGA
Garcia, G. E., & Stadtman, T. C. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.6.2093-2098.1991 · Cited by 47 · see citing works
Mechanism of action of clostridial glycine reductase: isolation and characterization of a covalent acetyl enzyme intermediate
Arkowitz, R. A., & Abeles, R. H. (1991) · Biochemistry · doi:10.1021/bi00230a039 · Cited by 45 · see citing works
Identification of acetylphosphate as the product of clostridial glycine reductase: evidence for an acyl enzyme intermediate
Arkowitz, R. A., & Abeles, R. H. (1989) · Biochemistry · doi:10.1021/bi00437a019 · Cited by 41 · see citing works
Breaking up is easy with esters
Perler, F. B. (1998) · Nature Structural Biology · doi:10.1038/nsb0498-249 · Cited by 40 · see citing works
Isolation and characterization of a covalent selenocysteine intermediate in the glycine reductase system
Arkowitz, R. A., & Abeles, R. H. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00158a059 · Cited by 39 · see citing works
Barriers to heterologous expression of a selenoprotein gene in bacteria
Tormay, P., & Böck, A. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.3.576-582.1997 · Cited by 39 · see citing works
Glycine Reductase of Clostridium Litorale
Kreimer, S., & Andreesen, J. R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.192_c.x · Cited by 35 · see citing works
Self-citation
Interaction of selenoprotein PA and the thioredoxin system, components of the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and Clostridium litorale [corrected]
Dietrichs, D., Meyer, M., Rieth, M., & Andreesen, J. R. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.19.5983-5991.1991 · Cited by 35 · see citing works
Self-citation
Clostridium sticklandii glycine reductase selenoprotein A gene: cloning, sequencing, and expression in Escherichia coli
Garcia, G. E., & Stadtman, T. C. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.22.7080-7089.1992 · Cited by 35 · see citing works
Enhanced in situ gel digestion of electrophoretically separated proteins with automated peptide elution onto mini reversed‐phase columns
Eckerskorn, C., & Grimm, R. (1996) · Electrophoresis · doi:10.1002/elps.1150170511 · Cited by 30 · see citing works
Self-citation
Selenoprotein A of the clostridial glycine reductase complex: purification and amino acid sequence of the selenocysteine-containing peptide.
Sliwkowski, M. X., & Stadtman, T. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.2.368 · Cited by 30 · see citing works
RNA Structures Involved in Selenoprotein SynthesisPreprint
Hüttenhofer, A., & Böck, A. (1998) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969509.35.603 · Cited by 29 · see citing works
Components of glycine reductase from Eubacterium acidaminophilum
Lübbers, M., & Andreesen, J. R. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18307.x · Cited by 26 · see citing works
Self-citation
Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum
SCHRÄDER, T., & Andreesen, J. R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16903.x · Cited by 25 · see citing works
Self-citation
Isolation of a cytochrome-deficient mutant strain of Sporomusa sphaeroides not capable of oxidizing methyl groups
Kamlage, B., & Blaut, M. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.10.3043-3050.1993 · Cited by 24 · see citing works
Glycine reductase protein C. Properties and characterization of its role in the reductive cleavage of Se-carboxymethyl-selenoprotein A.
Stadtman, T. C., & Davis, J. N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54546-4 · Cited by 22 · see citing works
Clostridial glycine reductase: protein C, the acetyl group acceptor, catalyzes the arsenate-dependent decomposition of acetyl phosphate.
Stadtman, T. C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7853 · Cited by 22 · see citing works
Thioredoxin elicits a new dihydrolipoamide dehydrogenase activity by interaction with the electron-transferring flavoprotein in Clostridium litoralis and Eubacterium acidaminophilum
Meyer, M., Dietrichs, D., Schmidt, B., & Andreesen, J. R. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.4.1509-1513.1991 · Cited by 18 · see citing works
Self-citation

Flagged first, then by citations

Research works printed but not linked: 2

Lu Èbbers, M. (1993) Klonierung, Sequenzierung und Analyse von Genen des Thioredoxin-Systems und der Glycin-Reduktase aus Eubacterium acidaminophilum. PhD Thesis, Go Èttingen.
Arkowitz, R.A. (1991) The mechanism of of action of clostridial glycine reductase: isolation and characterization of two covalent intermedi- ates. PhD Thesis, Brandeis University.

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Self-citation
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Gladyshev, V. N. (2007) · Springer eBooks · doi:10.1007/0-387-33827-6_9 · Cited by 22 · see citing works
Protein-derived cofactors: chemical innovations expanding enzyme catalysis
Graciano, A., & Liu, A. (2025) · Chemical Society Reviews · doi:10.1039/d4cs00981a · Cited by 19 · see citing works
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Staicu, L. C., Oremland, R. S., Tobe, R., & Mihara, H. (2017) · Plant ecophysiology · doi:10.1007/978-3-319-56249-0_6 · Cited by 17 · see citing works
Identity, evolution and function of selenoproteins and selenoprotein genes
Gladyshev, V. N. (2001) · Springer eBooks · doi:10.1007/978-1-4615-1609-5_9 · Cited by 17 · see citing works
Biological and Biochemical Aspects of Selenium Compounds
Bhuyan, B. J., & Mugesh, G. (2011) · Wiley eBooks · doi:10.1002/9783527641949.ch9 · Cited by 17 · see citing works
The Chemistry of Selenocysteine
Metanis, N., Beld, J., & Hilvert, D. (2011) · Patai's chemistry of functional groups · doi:10.1002/9780470682531.pat0582 · Cited by 16 · see citing works
Synthetic strategies for polypeptides and proteins by chemical ligation
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Selenium Proteins Containing Selenocysteine
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Arginine impacts aggregation, biofilm formation, and antibiotic susceptibility in Enterococcus faecalis
Snell, A. P., Manias, D. A., El-Behery, R. R., Dunny, G. M., & Willett, J. L. E. (2024) · FEMS Microbes · doi:10.1093/femsmc/xtae030 · Cited by 14 · see citing works
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Cys359 of GrdD is the active‐site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum
Kohlstock, U.-M., Rücknagel, K. P., Reuter, M., Schierhorn, A., Andreesen, J. R., & Söhling, B. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02590.x · Cited by 8 · see citing works
Self-citation
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Prokaryotic Selenoproteins and Selenoproteomes
Zhang, Y. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_12 · Cited by 5 · see citing works
Peroxidase activity of selenoprotein GrdB of glycine reductase and stabilisation of its integrity by components of proprotein GrdE from Eubacterium acidaminophilum
Gröbe, T., Reuter, M., Gursinsky, T., Söhling, B., & Andreesen, J. R. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0169-6 · Cited by 5 · see citing works
Self-citation
Selenocysteine as a Probe of Oxidative Protein Folding
Beld, J., Woycechowsky, K. J., & Hilvert, D. (2008) · Royal Society of Chemistry eBooks · doi:10.1039/9781847559265-00253 · Cited by 3 · see citing works
Selenium-Dependent Enzymes from Clostridia
Self, W. T. (2006) · Springer eBooks · doi:10.1007/0-387-22731-8_12 · Cited by 3 · see citing works
Protein-Derived Cofactors
Davidson, V. L. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00143-x · Cited by 3 · see citing works
Enzyme Mimetic Chemistry of Organoselenium Compounds
Bhowmick, D., & Mugesh, G. (2013) · Patai's chemistry of functional groups · doi:10.1002/9780470682531.pat0726 · Cited by 3 · see citing works
Protein-Derived Cofactors
Davidson, V. L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14615-3 · Cited by 2 · see citing works
The Physiology and Evolution of Selenite Respiration in Bacteria
Wells, M. (2020) · Cited by 1 · see citing works
Characterization of Microbials in the Lung Induced by Allergenic Platanus Pollen Protein (Pla a3) and Ambient Fine Particulate Matter
Liu, J., Lü, S., Hou, G., Hu, W., Zhao, J., Zhang, W., Liu, X., Enyoh, C. E., Wang, W., & Wang, Q. (2024) · Atmosphere · doi:10.3390/atmos15040503 · Cited by 1 · see citing works
Etude de la résistance de Cupriavidus metallidurans CH34 aux oxyanions sélénite et séléniate : accumulation, localisation et transformation du sélénium.
Avoscan, L. (2007) · HAL · Cited by 1 · see citing works
Selenium Proteins Containing SelenocysteineUpdate based on the original article by August Böck,Encyclopedia of Inorganic ChemistrySecond Edition, © 2005, John Wiley & Sons, Ltd.
Self, W. T. (2012) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0199.pub2
Peer Review #2 of "Whole genome sequencing of a novel, dichloromethane-fermenting Peptococcaceae from an enrichment culture (v0.2)"
(2019) · PeerJ · doi:10.7287/peerj.7775v0.2/reviews/2
Peer Review #2 of "Whole genome sequencing of a novel, dichloromethane-fermenting Peptococcaceae from an enrichment culture (v0.1)"
(2019) · PeerJ · doi:10.7287/peerj.7775v0.1/reviews/2
Glycine reductase
(2008) · Springer eBooks · doi:10.1007/3-540-30439-8_105
Sarcosine reductase
(2008) · Springer eBooks · doi:10.1007/3-540-30439-8_106
Functional Mimics of Glutathione Peroxidase: Spirochalcogenuranes, Mechanism and Its Antioxidant Activity
Lamani, D. S. (2022) · IntechOpen eBooks · doi:10.5772/intechopen.102430
Peer Review #1 of "Whole genome sequencing of a novel, dichloromethane-fermenting Peptococcaceae from an enrichment culture (v0.1)"
(2019) · PeerJ · doi:10.7287/peerj.7775v0.1/reviews/1
Peer Review #1 of "Whole genome sequencing of a novel, dichloromethane-fermenting Peptococcaceae from an enrichment culture (v0.2)"
(2019) · PeerJ · doi:10.7287/peerj.7775v0.2/reviews/1
betaine reductase
Schomburg, P. D., & Schomburg, D. I. (2008) · Springer eBooks · doi:10.1007/3-540-30439-8_107

Peroxidase activity of selenoprotein GrdB of glycine reductase and stabilisation of its integrity by components of proprotein GrdE from Eubacterium acidaminophilum
Gröbe, T., Reuter, M., Gursinsky, T., Söhling, B., & Andreesen, J. R. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0169-6 · Cited by 5 · see citing works
Self-citation
Glycine Reductase of Clostridium Litorale
Kreimer, S., & Andreesen, J. R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.192_c.x · Cited by 35 · see citing works
Self-citation
Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum
SCHRÄDER, T., & Andreesen, J. R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16903.x · Cited by 25 · see citing works
Self-citation
Purification and Characterization of Protein PB of Betaine Reductase and its Relationship to the Corresponding Proteins Glycine Reductase and Sarcosine Reductase from Eubacterium Acidaminophilum
Meyer, M., Granderath, K., & Andreesen, J. R. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.184_c.x · Cited by 51 · see citing works
Self-citation
Components of glycine reductase from Eubacterium acidaminophilum
Lübbers, M., & Andreesen, J. R. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18307.x · Cited by 26 · see citing works
Self-citation

Authors: Wagner, M., Sonntag, D., Grimm, R., Pich, A., Eckerskorn, C., Söhling, B., & Andreesen, J. R.
Affiliations: Martin Luther University Halle-Wittenberg (DE)
Max Planck Institute of Biochemistry (DE)
ORCID: Wagner, Matthias
Pich, Andreas
Venue: European Journal of Biochemistry
Publisher: Wiley
Published: 1999-02-05
Volume: 260
Issue: 1
Pages: 38-49
ISSN: 0014-2956 (ISSN-L)
1432-1033
DOI: 10.1046/j.1432-1327.1999.00107.x
OpenAlex: W1600998909
Cited by: 74
References: 57
Citations by year: 2025: 2 · 2024: 2 · 2023: 4 · 2022: 1 · 2021: 2 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 3 · 2016: 1 · 2015: 3 · 2013: 2 · 2012: 1
FWCI: 4.74
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1054 d)
Locations: European Journal of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft
Max-Planck-Gesellschaft
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Organoselenium and organotellurium chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: glycine reductase, protein subunit composition, UGA codon, gene cloning, enzyme purification
MeSH terms: Amino Acid Oxidoreductases, Amino Acid Sequence, Bacterial Proteins, Base Sequence, Cell Division, Cloning, Molecular, Eubacterium, Genes, Bacterial, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Proteins, Selenium Radioisotopes, Substrate Specificity, Sequence Alignment, Sequence Analysis, DNA, Selenoproteins

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Substrate‐specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum: Biochemical and molecular analysis

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