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Information on EC 1.21.4.2 - glycine reductase and Organism(s) Acetoanaerobium sticklandii and UniProt Accession P26971
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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
-
selenium-dependent
- purinolyticum
-
selenocysteine-containing
- d-proline
-
opal
-
selenols
-
selenoenzymes
-
selenoether
- sporogenes
-
selenium-containing
- cylindrosporum
The taxonomic range for the selected organisms is: Acetoanaerobium sticklandii
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
mechanism
-
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
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acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
a selenium-containing protein, selenoprotein, is essential component of the enzyme
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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 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
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
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
-
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
-
-
-
?
additional information
?
-
-
Se-carboxymethyl selenprotein A is a substrate of protein C
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
-
-
-
-
?
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
glycine + phosphate + thioredoxin
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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
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
-
-
-
?
glycine + phosphate + thioredoxin
acetyl phosphate + NH3 + thioredoxin disulfide + H2O
-
conservation of energy as acetyl phosphate
-
-
?
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
-
conservation of energy as acetyl phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
required for decomposition of acetyl phosphate by protein C
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
inhibits the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate
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%
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
KCl
-
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited
additional information
-
inactivation of selenoprotein A from Clostridium purinolyticum by sheep antibodies elicited to selenoprotein A from Clostridium stricklandii
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiols
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such as dithiothreitol required for decomposition of acetyl phosphate by protein C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21162
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
26295
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
additional information
-
molecular mass is depending on the salt concentration present
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
selenoprotein B, alpha,beta, 1 * 21162 + 1 * 26295, mass spectroscopy, amino acid sequence
monomer
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)
monomer
-
selenoprotein A, 1* 25000 Da, but the two selenoproteins differ in amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
-
selenoprotein A component of enzyme is not a glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
-
30% loss of activity of protein C after heating for 10 min, at pH 7.0, in the presence of EDTA, with and without Mg2+
68
-
80% loss of activity of protein C after heating for 10 min, at pH 7.0, in the presence of EDTA, with and without Mg2+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited by alkylation selenoprotein A alkylated at pH 6 with bromoacetate is active as a component of the enzyme complex
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the pyruvoyl group-forming proproteins grdE, expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
Acetoanaerobium sticklandii, Gottschalkia purinilytica
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
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
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
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
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
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