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EC Tree
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.
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
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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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P-protein
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glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
mechanism
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glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
H-protein ping-pong mechanism
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glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
sequential random bi bi mechanism in which no abortive dead end complex is formed
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decarboxylation
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decarboxylation
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co-substrate is H-protein, a lipoid acid-containing protein
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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.
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
additional information
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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reaction is stimulated by lipoic acid which is a functional group of the H-protein
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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glycine decarboxylation catalyzed by P-protein alone is extremely low
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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lipoyl protein: H-protein, lipoamide can also act as acceptor
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additional information
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P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein
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additional information
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P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein
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additional information
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the glycine cleavage system consists of 4 protein components: 1. P-protein is a pyridoxal containing protein: a Schiff base is formed between the hydroxyl group of the pyridoxal phosphate and the alpha-NH2 of glycine, the amino group and the alpha-carbon of the glycine are transferred to the lipoamide cofactor of the second enzyme of the complex the H-protein, the alpha-carbonyl group of glycine is lost as CO2, 2. H-protein, 3. T-protein: catalyzes the passage of alpha-carbon from lipoamide of H protein to tetrahydrofolate, alpha-NH2 from glycine is lost as NH4+, 4. L-protein: catalyzes oxidation of reduced lipoamide back to its original form with concomitant reduction of NAD+ to NADH
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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reaction is stimulated by lipoic acid which is a functional group of the H-protein
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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glycine decarboxylation catalyzed by P-protein alone is extremely low
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glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
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lipoyl protein: H-protein, lipoamide can also act as acceptor
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pyridoxal 5'-phosphate
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pyridoxal phosphate binding site
pyridoxal 5'-phosphate
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bound
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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
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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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
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3.4
CO2
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glycine-CO2 exchange
0.0034
glycine
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20
glycine
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glycine-CO2 exchange
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6.6
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glycine-CO2 exchange
7.1
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glycine + lipoylprotein
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UniProt
brenda
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brenda
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brenda
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brenda
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physiological function
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part of glycine cleavage system
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GCSP_CHICK
1004
0
111852
Swiss-Prot
Mitochondrion (Reliability: 2 )
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100000
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alpha2, 2 * 100000, SDS-PAGE
208000
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sucrose density gradient centrifugation
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dimer
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alpha2, 2 * 100000, SDS-PAGE
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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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda