Information on EC 1.21.4.2 - glycine reductase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.21.4.2
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RECOMMENDED NAME
GeneOntology No.
glycine reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
purine metabolism
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purine nucleobases degradation I (anaerobic)
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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 hide
39307-24-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
in Brachyspira pilosicoli glycine reductase is part of a glycine reductase complex system consisting of cluster of nine genes
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Manually annotated by BRENDA team
strain HF, DSM 519T from DSMZ
SwissProt
Manually annotated by BRENDA team
strain al-2
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Manually annotated by BRENDA team
selenium-containing subunit GrdA
UniProt
Manually annotated by BRENDA team
three protein system consisting of proteins A,B, and C
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Manually annotated by BRENDA team
strain CDK
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl phosphate + ammonia + thioredoxin disulfide
glycine + phosphate + thioredoxin
show the reaction diagram
dithiothreitol + cumene hydroperoxide
?
show the reaction diagram
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peroxidase activity of enzyme
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?
glycine + phosphate + thioredoxin
acetyl phosphate + ammonia + thioredoxin disulfide
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl phosphate + ammonia + thioredoxin disulfide
glycine + phosphate + thioredoxin
show the reaction diagram
glycine + phosphate + thioredoxin
acetyl phosphate + ammonia + thioredoxin disulfide
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
acetyl phosphate
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inhibits protein C activity, although a substrate
Bromoacetate
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75Se-labeled protein A preparation is inactivated at pH 6, 25C, for 10 min in presence of 10 mM bromoacetate by about 25%
iodoacetate
KBH4
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inactivates protein B, very little effect on fraction C
KCl
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the ability of protein component C to catalyse the arsenate-dependent decomposition of acetyl phosphate is inhibited
NH2OH
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inhibits protein B and fraction C
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenate
thiols
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
5.5
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protein B of enzyme
51.3
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protein C of enzyme
352
substrate-specific selenoprotein B of enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
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of the arsenate dependent decomposition of acetyl phosphate, piperazin buffer
additional information
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pI of protein component C: 5.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 22
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peroxidase activity assay at
40
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of the arsenate dependent decomposition of acetyl phosphate
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000 - 240000
420000
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protein component C, gel filtration
additional information
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molecular mass is depending on the salt concentration present
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
selenoprotein B, alpha,beta,gamma, 2 * 22000 + 2 * 25000 + 2 * 47000
monomer
multimer
octamer
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protein C, alpha,beta, 4 * 57000 + 4 * 48000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
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selenoprotein A component of enzyme is not a glycoprotein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47
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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+
62 - 64
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protein C inactivated
68
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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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, no significant loss of activity during storage
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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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of protein C of enzyme
of protein C of enzyme, recombinant enzyme
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of pyruvoyl group-forming protein grdE
of selenoprotein A of enzyme
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of selenoprotein B of enzyme
of selenoprotein component PA by 75Se incorporation
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 selenocystein-containing protein A: grdA and substrate-specific selenoprotein B: grdB
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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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of the pyruvoyl group-forming proproteins grdE, expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of proline inhibits transcription of the grd operon encoding glycine reductase. Protein PrdR negatively regulates transcription of the glycine reductase-encoding genes in the presence of proline
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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no cleavage on the N-terminal side of a cysteine
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C242S
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cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
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C242T
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cleavage on the N-terminal side of a cysteine under similar conditions with more extended half-times than wild-type enzyme
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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
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mutation of potentially redox-active motif UxxCxxC results in still significant, but decreased peroxidase activity; 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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
denaturation with SDS and 2-mercaptoethanol for 15 min at 100C does not lead to degradation of protein PA
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