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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
?
-
Substrates: peroxidase activity of enzyme
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
additional information
?
-
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: reduction of glycine action is coupled with formation of ATP from ADP
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: enzyme activity is NADPH-dependent but not dithioerythritol-dependent
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: -
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
additional information
?
-
-
Substrates: Se-carboxymethyl selenprotein A is a substrate of protein C
Products: -
?
additional information
?
-
-
Substrates: Se-carboxymethyl selenprotein A is a substrate of protein C
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
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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
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
Substrates: -
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
Substrates: conservation of energy as acetyl phosphate
Products: -
?
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acetyl phosphate
-
inhibits protein C activity, although a substrate
Bromoacetate
-
75Se-labeled protein A preparation is inactivated at pH 6, 25°C, for 10 min in presence of 10 mM bromoacetate by about 25%
KBH4
-
inactivates protein B, very little effect on fraction C
KCl
-
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited
NH2OH
-
inhibits protein B and fraction C
(NH4)2SO4
-
inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate
(NH4)2SO4
-
70% loss of activity at 300 mM; inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate
iodoacetate
-
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited, but protein C is protected from inactivation by treatment acetyl phosphate
iodoacetate
-
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited, but protein C is protected from inactivation by treatment acetyl phosphate
additional information
-
no effect: CaCl2, CoCl2, MnCl2
-
additional information
-
inactivation of selenoprotein A from Clostridium purinolyticum by sheep antibodies elicited to selenoprotein A from Clostridium stricklandii
-
additional information
-
inactivation of selenoprotein A from Clostridium purinolyticum by sheep antibodies elicited to selenoprotein A from Clostridium stricklandii
-
additional information
-
antibodies raised against the thioredoxin reductase-like flavoprotein or thioredoxin inhibit to a high extent
-
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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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C242A
no cleavage on the N-terminal side of a cysteine
C242S
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
C242T
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
C242A
-
no cleavage on the N-terminal side of a cysteine
-
C242S
-
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
-
C242T
-
cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
-
C353
-
mutation of potentially redox-active motif UxxCxxC, 44% of wild-type peroxidase activity
C356
-
mutation of potentially redox-active motif UxxCxxC, 40% of wild-type peroxidase activity
C359A
-
grdD of protein component C, mutant enzyme completely inactive, accessible to iodoacetate only under native conditions, suggesting that Cys359 of GrdD is the thiol responsible for the formation of the acetyl thioester during catalysis of arsenate-dependent hydrolysis of acetyl phosphate
C98S
-
grdD of protein component C, activity is unchanged, accessible to iodoacetate only after denaturation
U350
-
mutation of potentially redox-active motif UxxCxxC, 60% of wild-type peroxidase activity
additional information
-
mutation of potentially redox-active motif UxxCxxC results in still significant, but decreased peroxidase activity
additional information
-
mutation of the potentially redox-active UxxCxxC motif in subunit GrdB of the B protein complex results in still signifiant, but decreased peroxidase activity, overview
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