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acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
mechanism
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
mechanism
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
mechanism
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
cleavage mechanism for the pyruvoyl group dependent reductase starting from cysteine
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
cleavage mechanism for the pyruvoyl group dependent reductase starting from cysteine
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
the protein C component catalyses the arsenate-dependent decomposition of acetyl phosphate
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
the protein C component catalyses the arsenate-dependent decomposition of acetyl phosphate
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
the protein component C serves as the acetyl group acceptor in the overall reaction
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
a selenium-containing protein, selenoprotein, is essential component of the enzyme
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
a selenium-containing protein, selenoprotein, is essential component of the enzyme
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
GrdD of protein component C catalyses the arsenate-dependent decomposition of acetyl phosphate, whereas GrdC completely inactive
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
Cys 359 of GrdD is the thiol responsible for the formation of the acetyl thioester during catalysis of arsenate-dependent hydrolysis of acetyl phosphate
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
the 48000 Da subunit of protein component C catalyses the arsenate-dependent decomposition of actetyl phosphate, a possible role of the 57000 Da subunit of protein component C could be the involvement in the reductive dehydration which leads to the cleavage of the protein A-bound carboxymethyl-selenoether to ketene and oxidized protein A
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
mechanism, thiols are present in protein C that is acetylated during reaction
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
the thioredoxin system is involved in the electron transport from reduced pyridine nucleotides to protein A, i.e. in the electron flow between protein of glycine decarboxylase and glycine reductase complex
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
glycine pathway is used for acetate synthesis
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
mechanism
-
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
cleavage mechanism for the pyruvoyl group dependent reductase starting from cysteine
-
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
The reaction is observed only in the direction of glycine reduction. The enzyme consists of three protein components A, B and C. Protein B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Protein A, which also contains selenocysteine, is reduced by thioredoxin, and is needed to convert the carboxymethyl group into a ketene equivalent, in turn used by protein C to produce acetyl phosphate. Only protein B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase)
-
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
glycine pathway is used for acetate synthesis
-
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
-
-
-
-
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acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
dithiothreitol + cumene hydroperoxide
?
-
peroxidase activity of enzyme
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
additional information
?
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
reduction of glycine action is coupled with formation of ATP from ADP
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
reduction of glycine action is coupled with formation of ATP from ADP
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
enzyme activity is NADPH-dependent but not dithioerythritol-dependent
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
additional information
?
-
-
Se-carboxymethyl selenprotein A is a substrate of protein C
-
-
?
additional information
?
-
-
Se-carboxymethyl selenprotein A is a substrate of protein C
-
-
?
additional information
?
-
-
the B protein complex, consisting of the selenocysteine-containing GrdB subunit and two subunits, which are derived from the GrdE proprotein, shows 1.7 U/mg peroxidase activity with DTT and cumene hydroperoxide as substrates, the protein exhibits DTT- as well as NADPH-dependent peroxidase activity, overview
-
-
?
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acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
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16700
-
selenoprotein A, 1 * 16700, amino acid sequence
17011
-
1 * 17011 calculated from amino acid sequence
17022
-
selenoprotein A, 1 * 17022, mass spectroscopy
18000
-
selenoprotein A, 1 * 18000
21162
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
22000
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
25000
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
26295
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
420000
-
protein component C, gel filtration
45000
-
selenoprotein B, 1 * 45000, SDS-PAGE
48000
-
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
57000
-
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
additional information
-
molecular mass is depending on the salt concentration present
18500
-
selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences
18500
-
selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences
200000 - 240000
-
protein C, gel filtration
200000 - 240000
-
protein C, gel filtration
200000 - 240000
-
protein C, gel filtration
40000
-
protein C, x * 40000 + x * 54000
40000
-
protein C, x * 40000 + x * 54000
40000
-
protein C, x * 40000 + x * 54000
47000
-
selenoprotein B, 1 * 47000, amino acid sequence
47000
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
54000
-
protein C, x * 40000 + x * 54000
54000
-
protein C, x * 40000 + x * 54000
54000
-
protein C, x * 40000 + x * 54000
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hexamer
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
octamer
-
protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
dimer
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
dimer
-
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
-
monomer
-
1 * 17011 calculated from amino acid sequence
monomer
-
selenoprotein A, 1 * 17022, mass spectroscopy
monomer
-
selenoprotein A, 1* 25000 Da, but the two selenoproteins differ in amino acid sequence
monomer
-
selenoprotein A, 1* 25000 Da, but the two selenoproteins differ in amino acid sequence
monomer
-
selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences
monomer
-
selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences
monomer
-
selenoprotein A, 1 * 16700, amino acid sequence
monomer
-
selenoprotein B, 1 * 47000, amino acid sequence
monomer
-
selenoprotein B, 1 * 45000, SDS-PAGE
monomer
-
selenoprotein A, 1 * 18000
monomer
-
selenoprotein B, 1 * 45000, SDS-PAGE
-
monomer
-
selenoprotein A, 1 * 18000
-
multimer
-
protein C, x * 40000 + x * 54000
multimer
-
protein C, x * 40000 + x * 54000
multimer
-
protein C, x * 40000 + x * 54000
additional information
-
three protein system consisting of protein A (17000 Da), protein B (47000 Da or 48000 Da, later processed into two proteins of 22000 and 25000 Da), and protein C (40000 or 54000 Da)
additional information
-
three protein system consisting of protein A (17000 Da), protein B (47000 Da or 48000 Da, later processed into two proteins of 22000 and 25000 Da), and protein C (40000 or 54000 Da)
additional information
-
heterologous enzyme is protected from degradation by full-length GrdE or by GrdE domains
additional information
-
the enzyme consists of three subunits A, B, and C. The protein B-complex consists of the selenocysteine-containing GrdB subunit, subunit B, and two subunits, which derive from the GrdE proprotein, one of which shows peroxidase activity and protects the sensitive selenoproteins in the organism
additional information
-
three protein system consisting of protein A (17000 Da), protein B (47000 Da or 48000 Da, later processed into two proteins of 22000 and 25000 Da), and protein C (40000 or 54000 Da)
additional information
-
three protein system consisting of protein A (17000 Da), protein B (47000 Da or 48000 Da, later processed into two proteins of 22000 and 25000 Da), and protein C (40000 or 54000 Da)
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Bednarski, B.; Andreesen, J.R.; Pich, A.
In vitro processing of the proproteins GrdE of protein B of glycine reductase and PrdA of D-proline reductase from Clostridium sticklandii: formation of a pyruvoyl group from a cysteine residue
Eur. J. Biochem.
268
3538-3544
2001
Acetoanaerobium sticklandii (P26971), Acetoanaerobium sticklandii, Acetoanaerobium sticklandii DSM 519 (P26971)
brenda
Wagner, M.; Sonntag, D.; Grimm, R.; Pich, A.; Eckerskorn, C.; Shling, B.; Andreesen, J.R.
Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum
Eur. J. Biochem.
260
38-49
1999
Peptoclostridium acidaminophilum (Q9R4G7), Peptoclostridium acidaminophilum
brenda
Tanaka, H.; Stadtman, T.C.
Selenium-dependent clostridial glycine reductase. Purification and characterization of the two membrane-associated protein components
J. Biol. Chem.
254
447-452
1979
Acetoanaerobium sticklandii
brenda
Sliwkowski, M.X.; Stadtman, T.C.
Selenium-dependent glycine reductase: differences in physicochemical properties and biological activities of selenoprotein A components isolated from Clostridium sticklandii and Clostridium purinolyticum
Biofactors
1
293-296
1988
Gottschalkia purinilytica, Acetoanaerobium sticklandii
brenda
Sliwkowski, M.X.; Stadtman, T.C.
Selenoprotein A of the clostridial glycine reductase complex: purification and amino acid sequence of the selenocysteine-containing peptide
Proc. Natl. Acad. Sci. USA
85
368-371
1988
Acetoanaerobium sticklandii
brenda
Stadtman, T.C.
Clostridial glycine reductase: protein C, the acetyl group acceptor, catalyzes the arsenate-dependent decomposition of acetyl phosphate
Proc. Natl. Acad. Sci. USA
86
7853-7856
1989
Acetoanaerobium sticklandii
brenda
Garcia, G.E.; Stadtman, T.C.
Selenoprotein A component of the glycine reductase complex from Clostridium purinolyticum: nucleotide sequence of the gene shows that selenocysteine is encoded by UGA
J. Bacteriol.
173
2093-2098
1991
Gottschalkia purinilytica
brenda
Stadtman, T.C.; Davis, J.N.
Glycine reductase protein C. Properties and characterization of its role in the reductive cleavage of Se-carboxymethyl-selenoprotein A
J. Biol. Chem.
266
22147-22153
1991
Acetoanaerobium sticklandii
brenda
Kimura, Y.; Stadtman, T.C.
Glycine reductase selenoprotein A is not a glycoprotein: the positive periodic acid-Schiff reagent test is the result of peptide bond cleavage and carbonyl group generation
Proc. Natl. Acad. Sci. USA
92
2189-2193
1995
Acetoanaerobium sticklandii
brenda
Dietrichs, D.; Meyer, M.; Rieth, M.; Andreesen, J.R.
Interaction of selenoprotein PA and the thioredoxin system, components of the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and Clostridium litorale. [Erratum to document cited in CA116(1):2789b]
J. Bacteriol.
173
5983-5991
1992
Peptoclostridium litorale, Peptoclostridium acidaminophilum
brenda
Schraeder, T.; Andreesen, J.R.
Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum
Eur. J. Biochem.
206
79-85
1992
Peptoclostridium acidaminophilum
brenda
Kohlstock, U.M.; Rucknagel, K.P.; Reuter, M.; Schierhorn, A.; Andreesen, J.R.; Sohling, B.
Cys359 of GrdD is the active-site thiol that catalyses the final step of acetyl phosphate formation by glycine reductase from Eubacterium acidaminophilum
Eur. J. Biochem.
268
6417-6425
2001
Peptoclostridium acidaminophilum
brenda
Kreimer, S.; Andreesen, J.R.
Glycine reductase of Clostridium littorale. Cloning, sequencing, and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation
Eur. J. Biochem.
234
192-199
1995
Peptoclostridium litorale
brenda
Schneeberger, A.; Frings, J.; Schink, B.
Net synthesis of acetate from CO2 by Eubacterium acidaminophilum through the glycine reductase pathway
FEMS Microbiol. Lett.
177
1-6
1999
Peptoclostridium acidaminophilum, Peptoclostridium acidaminophilum al-2
-
brenda
Arkowitz, R.A.; Abeles, R.H.
Mechanism of action of clostridial glycine reductase: isolation and characterization of a covalent acetyl enzyme intermediate
Biochemistry
30
4090-4097
1991
Acetoanaerobium sticklandii
brenda
Rother, M.; Bock, A.; Wyss, C.
Selenium-dependent growth of Treponema denticola: evidence for a clostridial-type glycine reductase
Arch. Microbiol.
177
113-116
2001
Treponema denticola, Treponema denticola CDK
brenda
Andreesen, J.R.
Glycine reductase mechanism
Curr. Opin. Chem. Biol.
8
454-461
2004
Acetoanaerobium sticklandii, Peptoclostridium acidaminophilum, Tissierella creatinophila, Treponema denticola
brenda
Groebe, T.; Reuter, M.; Gursinsky, T.; Soehling, B.; Andreesen, J.R.
Peroxidase activity of selenoprotein GrdB of glycine reductase and stabilisation of its integrity by components of proprotein GrdE from Eubacterium acidaminophilum
Arch. Microbiol.
187
29-43
2007
Peptoclostridium acidaminophilum
brenda
Jackson, S.; Calos, M.; Myers, A.; Self, W.T.
Analysis of proline reduction in the nosocomial pathogen Clostridium difficile
J. Bacteriol.
188
8487-8495
2006
Clostridioides difficile
brenda
Wanchanthuek, P.; Bellgard, M.; La, T.; Ryan, K.; Moolhuijzen, P.; Chapman, B.; Black, M.; Schibeci, D.; Hunter, A.; Barrero, R.; Phillips, N.; Hampson, D.
The complete genome sequence of the pathogenic intestinal spirochete Brachyspira pilosicoli and comparison with other Brachyspira genomes
PLoS ONE
5
e11455
2010
Brachyspira pilosicoli
brenda
Bouillaut, L.; Self, W.T.; Sonenshein, A.L.
Proline-dependent regulation of Clostridium difficile Stickland metabolism
J. Bacteriol.
195
844-854
2013
Clostridioides difficile (Q185M6), Clostridioides difficile, Clostridioides difficile 630 (Q185M6)
brenda