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Information on EC 1.21.4.2 - glycine reductase and Organism(s) Peptoclostridium acidaminophilum and UniProt Accession Q9R4G7
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1.21.4.2 glycine reductaseIUBMB Comments
The reaction is observed only in the direction of glycine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Subunit 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 subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase).
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Word Map
- 1.21.4.2
- selenocysteine
-
clostridial
- sticklandii
- eubacterium
- acidaminophilum
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selenium-dependent
- purinolyticum
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selenocysteine-containing
- d-proline
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opal
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selenols
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selenoenzymes
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selenoether
- sporogenes
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selenium-containing
- cylindrosporum
The taxonomic range for the selected organisms is: Peptoclostridium acidaminophilum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glycine reductase, 
more
topREACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
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
the protein C component catalyses the arsenate-dependent decomposition of acetyl phosphate
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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
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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
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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
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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
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acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
glycine pathway is used for acetate synthesis
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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)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
-
-
-
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reduction
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-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-phosphate ammonia:thioredoxin disulfide oxidoreductase (glycine-forming)
The reaction is observed only in the direction of glycine reduction. The enzyme from Eubacterium acidaminophilum consists of subunits A, B and C. Subunit B contains selenocysteine and a pyruvoyl group, and is responsible for glycine binding and ammonia release. Subunit 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 subunit C to produce acetyl phosphate. Only subunit B distinguishes this enzyme from EC 1.21.4.3 (sarcosine reductase) and EC 1.21.4.4 (betaine reductase).
CAS REGISTRY NUMBER
COMMENTARY
39307-24-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
?
dithiothreitol + cumene hydroperoxide
?
-
peroxidase activity of enzyme
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
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-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
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enzyme activity is NADPH-dependent but not dithioerythritol-dependent
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-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
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-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
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conservation of energy as acetyl phosphate
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-
?
additional information
?
-
-
Se-carboxymethyl selenprotein A is a substrate of protein C
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-
?
additional information
?
-
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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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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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conservation of energy as acetyl phosphate
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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not absolutely required, but increases activity by about 20%, the highest enzyme activity in presence of 10 mM MgCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl phosphate
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inhibits protein C activity, although a substrate
iodoacetate
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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
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antibodies raised against the thioredoxin reductase-like flavoprotein or thioredoxin inhibit to a high extent
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(NH4)2SO4
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inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiols
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not absolutely required, but increases activity by about 20%, the highest enzyme activity in presence of 10 mM dithioerythritol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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kinetics of the DTT-dependent peroxidase activity of the protein B complex
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the protein B complex shows 1.7 U/mg peroxidase activity with DTT and cumene hydroperoxide as substrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
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of the arsenate dependent decomposition of acetyl phosphate, piperazin buffer
7.5
7.5
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of the arsenate dependent decomposition of acetyl phosphate, Tris/HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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of the arsenate dependent decomposition of acetyl phosphate
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
25000
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
47000
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
18500
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selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences
48000
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protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
57000
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protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
monomer
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selenoprotein A, 1 * 18500, SDS-PAGE, the two selenoproteins exhibit very similar N-terminal amino acid sequences
octamer
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protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
additional information
additional information
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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
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heterologous enzyme is protected from degradation by full-length GrdE or by GrdE domains
additional information
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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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C353
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mutation of potentially redox-active motif UxxCxxC, 44% of wild-type peroxidase activity
C356
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mutation of potentially redox-active motif UxxCxxC, 40% of wild-type peroxidase activity
C359A
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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
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grdD of protein component C, activity is unchanged, accessible to iodoacetate only after denaturation
U350
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mutation of potentially redox-active motif UxxCxxC, 60% of wild-type peroxidase activity
additional information
additional information
-
mutation of potentially redox-active motif UxxCxxC results in still significant, but decreased peroxidase activity
additional information
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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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of recombinant GrdE with recombinant Strep-tagged GrdB, native DTT-dependent peroxidase activity 14fold by anion exchange and hydrophobic interaction chromatography, ammonium sulfate fractionation, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and sequencing of a new gene region, encoding a proprotein for the beta and alpha subunits of selenoprotein B: grdE, selenoprotein A: grdA and selenium-containing gamma subunit of selenoprotein B: grdB
cloning of two subunits of protein C: grdC1 and grdD1, expression in Escherichia coli
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expression of wild-type and mutant B protein complex components in Escherichia coli strain XL1-Blue
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation with SDS and 2-mercaptoethanol for 15 min at 100°C does not lead to degradation of protein PA
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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 acidaminophilum, Peptoclostridium litorale
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
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
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
-
Andreesen, J.R.
Glycine reductase mechanism
Curr. Opin. Chem. Biol.
8
454-461
2004
Acetoanaerobium sticklandii, Peptoclostridium acidaminophilum, Tissierella creatinophila, Treponema denticola
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
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