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Information on EC 1.4.4.2 - glycine dehydrogenase (aminomethyl-transferring) and Organism(s) Gallus gallus and UniProt Accession P15505

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IUBMB Comments
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein . Previously known as glycine synthase.
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Gallus gallus
UNIPROT: P15505
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The taxonomic range for the selected organisms is: Gallus gallus
The enzyme appears in selected viruses and cellular organisms
Synonyms
gdc, h protein, h-protein, glycine decarboxylase, t protein, protein p1, h1 protein, glycine decarboxylase complex, glycine cleavage enzyme complex, h2 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylase, glycine
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Glycine cleavage system P-protein
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glycine decarboxylase
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glycine decarboxylase P-protein
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glycine dehydrogenase
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glycine dehydrogenase (decarboxylating)
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glycine-cleavage complex
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-
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P-protein
Protein P1
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating)
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein [3]. Previously known as glycine synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
37259-67-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
show the reaction diagram
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-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
show the reaction diagram
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CO2
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product inhibition
Co2+
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inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Cu2+
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inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Fe2+
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slight inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Glycine methyl ester
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K2HPO4
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inhibition of glycine-CO2 exchange reaction
KCl
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inhibition of glycine-CO2 exchange reaction
Modified H-protein
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lipoic acid prosthetic group and cysteinyl residues modified with N-ethylmaleimide
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N4-methylglutamine
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inhibition of glycine-CO2 exchange reaction
Ni2+
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inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Zn2+
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inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
additional information
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inactivation after incubation with glycine in presence of aminomethyl carrier protein (H-protein), it is a suicide reaction of the P-protein as a side reaction of the glycine decarboxylation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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thiol compound required for maximal activity on glycine-CO2 exchange reaction
dithiothreitol
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thiol compound required for maximal activity on glycine-CO2 exchange reaction
GSH
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thiol compound required for maximal activity on glycine-CO2 exchange reaction
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.4
CO2
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glycine-CO2 exchange
0.0034 - 40
glycine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
-
glycine-CO2 exchange
7.1
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glycine + lipoylprotein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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part of glycine cleavage system
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GCSP_CHICK
1004
0
111852
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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alpha2, 2 * 100000, SDS-PAGE
200000
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value about
208000
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sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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alpha2, 2 * 100000, SDS-PAGE
homodimer
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several weeks
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiraga, K.; Kikuchi, G.
The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria
J. Biol. Chem.
255
11664-11670
1980
Gallus gallus
Manually annotated by BRENDA team
Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y.
Amino acid sequence of the phosphopyridoxyl peptide from P-protein of the chicken liver glycine cleavage system
Biochem. Biophys. Res. Commun.
149
621-627
1987
Gallus gallus
Manually annotated by BRENDA team
Fujiwara, K.; Okamura-Ikeda, K.; Ohmura, Y.; Motokawa, Y.
Mechanism of the glycine cleavage reaction: retention of C-2 hydrogens of glycine on the intermediate attached to H-protein and evidence for the inability of serine hydroxymethyltransferase to catalyze the glycine decarboxylation
Arch. Biochem. Biophys.
251
121-127
1986
Bos taurus, Gallus gallus
Manually annotated by BRENDA team
Fujiwara, K.; Motokawa, Y.
Mechanism of the glycine cleavage reaction. Steady state kinetic studies of the P-protein-catalyzed reaction
J. Biol. Chem.
258
8156-8162
1983
Gallus gallus
Manually annotated by BRENDA team
Hiraga, K.; Kikuchi, G.
The mitochondrial glycine cleavage system: inactivation of glycine decarboxylase as a side reaction of the glycine decarboxylation in the presence of aminomethyl carrier protein
J. Biochem.
92
1489-1498
1982
Gallus gallus
Manually annotated by BRENDA team
Hiraga, K.; Kikuchi, G.
The mitochondrial glycine cleavage system: differential inhibition by divalent cations of glycine synthesis and glycine decarboxylation in the glycine-CO2 exchange
J. Biochem.
92
937-944
1982
Gallus gallus
Manually annotated by BRENDA team
Hiraga, K.; Kikuchi, G.
The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein
J. Biol. Chem.
255
11671-11676
1980
Gallus gallus
Manually annotated by BRENDA team
Kawaguchi, H.; Okamoto, S.; Sikdar, D.; Kume, A.; Li, F.; Mohafez, O.M.; Shehata, M.H.; Hiraga, K.
Genomic organization of regions that regulate chicken glycine decarboxylase gene transcription: physiological and pathological implications
Gene
432
7-18
2009
Gallus gallus (P15505), Gallus gallus
Manually annotated by BRENDA team
Kikuchi, G.; Motokawa, Y.; Yoshida, T.; Hiraga, K.
Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia
Proc. Jpn. Acad. Ser. B Phys. Biol. Sci.
84
246-263
2008
Gallus gallus, Gottschalkia acidurici, Escherichia coli, Peptoclostridium acidaminophilum, Thermus thermophilus, Homo sapiens, Pisum sativum
Manually annotated by BRENDA team