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decarboxylase, glycine
-
-
-
-
GLDP
-
serves as the actual decarboxylating unit of GDC
Gly decarboxylase complex
-
-
glycine cleavage enzyme complex
-
glycine cleavage H protein
-
-
glycine cleavage system H protein 1
-
Glycine cleavage system P-protein
-
-
-
-
glycine decarboxylase (P-protein)
glycine decarboxylase complex
glycine decarboxylase complex H
-
glycine decarboxylase P-protein
-
-
-
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glycine dehydrogenase (decarboxylating)
-
-
-
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glycine-cleavage complex
-
-
-
-
P-protein (glycine decarboxylase)
-
-
P-subunit
-
serves as the actual decarboxylating unit of GDC
additional information
glycine decarboxylase, or P-protein, is part of the glycine cleavage system, GCS
GDC
-
-
GDC
-
a four-protein system comprising three enzymes (P-protein, T-protein, and L-protein) plus H-protein
GDC
GDC is composed of four subunits, designated P-, H-, T-, and L-proteins, encoded by nuclear genes with N-terminal mitochondrial targeting pre-sequences, the Populus genome contains eight transcriptionally active GDC genes, encoding four H-proteins, two T-proteins, and single P- and L-proteins
GLDC
-
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glycine decarboxylase
-
-
-
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glycine decarboxylase
-
-
glycine decarboxylase
-
-
glycine decarboxylase
-
-
glycine decarboxylase
-
-
glycine decarboxylase
-
-
glycine decarboxylase (P-protein)
-
-
glycine decarboxylase (P-protein)
-
-
-
glycine decarboxylase complex
-
glycine decarboxylase complex
the glycine decarboxylase complex cooperates with serine hydroxymethyltransferase to mediate photorespiratory glycine-serine interconversion
glycine decarboxylase complex
-
-
glycine decarboxylase complex
-
-
glycine decarboxylase complex
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glycine decarboxylase complex
-
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glycine dehydrogenase
-
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glycine dehydrogenase
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-
glycine dehydrogenase
-
-
glycine dehydrogenase
-
-
glycine dehydrogenase
-
-
glycine dehydrogenase
-
-
glycine dehydrogenase
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-
glycine dehydrogenase
-
-
glycine dehydrogenase
-
-
P protein
-
-
P-protein
-
-
-
-
P-protein
-
part of the glycine cleavage system
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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
-
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
mechanism
-
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
-
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
-
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
mechanism of the GLDC-catalyzed reaction, detailed overview. GLDC is an unusual PLP-containing alpha-amino acid decarboxylase that removes carbon dioxide from the glycine substrate without releasing the expected amine (methylamine, a metabolic precursor of toxic formaldehyde) as a product. In an unusual decarboxylation mechanism, the resulting aminomethyl moiety is instead transferred to an accessory H-protein. (1) H-Protein is not required for glycine decarboxylation but, instead, is required for the release of the aminomethyl moiety from the quinonoid adduct. (2) Glycine decarboxylation is reversible and presumably proceeds through a stable quinonoid intermediate. (3) The physiological product of glycine decarboxylation is H-protein-S-aminomethyl dihydrolipoyllysine and not methylamine (in the absence of H-protein, the aminomethyl moiety remains as a quinonoid adduct)
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
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-
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glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
glycine + His-tagged H-apoprotein
?
-
very low activity
-
-
?
glycine + lipoamide
?
-
-
-
-
?
glycine + lipoate
?
-
very low activity
-
-
?
glycine + lipoylated H-apoprotein
?
-
very low activity
-
-
?
glycine + lipoylated His-tagged H-apoprotein
?
-
very low activity
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
glycine + rTvH1 protein
?
-
-
-
-
?
glycine + rTvH2 protein
?
-
-
-
-
?
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
H1 protein
?
-
substrate for L protein
-
-
?
H2 protein
?
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substrate for L protein
-
-
?
P2 protein-S-aminomethyldihydrolipoyl-L-lysine + bicarbonate
?
-
-
-
-
r
additional information
?
-
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor. CO2 is released in the reaction and the residual aminomethyl group is bound to the oxidized lipoamide arm of H-protein
the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
C3-plants
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-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
reaction is stimulated by lipoic acid which is a functional group of the H-protein
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
glycine decarboxylation catalyzed by P-protein alone is extremely low
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
-
?
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
-
-
-
r
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
reversible reaction
-
-
r
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the GDC H-protein (GLDH) has no catalytic activity itself but interacts via its lipoyl arm one after the other with the three other GDC subunits, P-protein (EC 1.4.4.2), T-protein (EC 2.1.2.10), and L-protein (EC 1.8.1.4)
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-
?
additional information
?
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the GDC H-protein is a substrate for P-protein of glycine decarboxylase
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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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-
?
additional information
?
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nonketotic hyperglycinaemia is an autosomal recessive disorder of glycine metabolism caused by a deficiency in the mitochondrial glycine cleavage enzyme. The majority of cases are caused by mutations in the P-protein
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-
?
additional information
?
-
presence of excess pyridoxal 5'-phosphate is used in the assay mixture to facilitate the displacement of the quinonoid intermediate in the absence of an acceptor for the methylamine moiety (of decarboxylated glycine) to allow multiple enzyme turnovers. Mass spectrometry and 13C NMR spectroscopy are used to determine the products of glycine decarboxylation. The assay reaction mixtures are incubated for 1 week at pH 7.0, 25°C
-
-
?
additional information
?
-
-
presence of excess pyridoxal 5'-phosphate is used in the assay mixture to facilitate the displacement of the quinonoid intermediate in the absence of an acceptor for the methylamine moiety (of decarboxylated glycine) to allow multiple enzyme turnovers. Mass spectrometry and 13C NMR spectroscopy are used to determine the products of glycine decarboxylation. The assay reaction mixtures are incubated for 1 week at pH 7.0, 25°C
-
-
?
additional information
?
-
-
glycine decarboxylase does not occur as a complex of all four proteins, but L-protein takes part in both glycine decarboxylase as well as in glycine reductase reaction
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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
-
-
?
additional information
?
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the enzyme is a component of the reversible glycine cleavage system, previously known as glycine synthase
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-
?
additional information
?
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in transgenic potato plants with an antisense reduction in P-protein of GDC, the decrease in photorespiratory decarboxylation is compensated for by an increase in respiratory decarboxylation in the light
-
-
?
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glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine
[glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2
-
-
-
r
additional information
?
-
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
P-protein is the actual glycine-decarboxylating enzyme and uses pyridoxal 5'-phosphate as a cofactor. CO2 is released in the reaction and the residual aminomethyl group is bound to the oxidized lipoamide arm of H-protein
the methylene group is accepted by tetrahydrofolate to yield methylene tetrahydrofolate, a major cofactor in one-carbon metabolism
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + H-protein-lipoyllysine
H-protein-S-aminomethyldihydrolipoyllysine + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
C3-plants
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
reaction is stimulated by lipoic acid which is a functional group of the H-protein
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
glycine decarboxylation catalyzed by P-protein alone is extremely low
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
-
-
-
?
glycine + lipoylprotein
S-aminomethyldihydrolipoylprotein + CO2
-
lipoyl protein: H-protein, lipoamide can also act as acceptor
-
-
?
additional information
?
-
-
nonketotic hyperglycinaemia is an autosomal recessive disorder of glycine metabolism caused by a deficiency in the mitochondrial glycine cleavage enzyme. The majority of cases are caused by mutations in the P-protein
-
-
?
additional information
?
-
-
in transgenic potato plants with an antisense reduction in P-protein of GDC, the decrease in photorespiratory decarboxylation is compensated for by an increase in respiratory decarboxylation in the light
-
-
?
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5,5'-dithiobis-(2-nitrobenzoic acid)
complete inhibition
aminoacetonitrile
the inhibitor of GDC is able to mimic mitochondrial depolarization, hydrogen peroxide production, and cell death in response to stress or harpin treatment of cultured Arabidopsis cells
Co2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Cu2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
Fe2+
-
slight inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
harpin
the bacterial elicitor, a strong inducer of reactive oxygen species and NO, inhibits GDC activity
-
K2HPO4
-
inhibition of glycine-CO2 exchange reaction
KCl
-
inhibition of glycine-CO2 exchange reaction
Modified H-protein
-
lipoic acid prosthetic group and cysteinyl residues modified with N-ethylmaleimide
-
N4-methylglutamine
-
inhibition of glycine-CO2 exchange reaction
Ni2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
S-nitrosoglutathione
i.e. GSNO, the glycine decarboxylase complex, GDC activity is inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues, overview. The inhibition of GDC activity after GSNO treatment can be an indirect effect of ROS induced by inhibition of complex I
serine
C3-plants
-
competitive inhibitor
Zn2+
-
inhibition of glycine-CO2 exchange by binding of metal with H-protein-bound intermediate of glycine decarboxylation
N-ethylmaleimide
complete inhibition
additional information
-
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
-
additional information
-
inhibitors of the multienzyme complex
-
additional information
-
inhibitors of the multienzyme complex
-
additional information
-
low CO2 concentrations decrease expression of GDC
-
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2-mercaptoethanol
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
GSH
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
H-protein
upon addition of exogenous unlipoylated H-protein, kcat increases 190fold, in the absence of the lipoic acid moiety on H-protein, the methylamine adduct with pyridoxal 5'-phosphate (aminomethyl-quinonoid intermediate) is released as the product of the GLDC-catalyzed decarboxylation of glycine
-
lipoylated H-protein
the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation
-
dithiothreitol
-
thiol compound required for maximal activity on glycine-CO2 exchange reaction
dithiothreitol
-
P and H protein alone jointly catalyze the glycine-CO2 exchange reaction in presence of pyridoxal phosphate and dithiothreitol
additional information
the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation further corroborates the suggestion that H-protein (or lipoylated H-protein) does not directly participate in and is not required for release of CO2 from glycine in the formation of the pyridoxal 5'-phosphate-quinonoid intermediate, an important distinction that is contrary to earlier findings
-
additional information
-
the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation further corroborates the suggestion that H-protein (or lipoylated H-protein) does not directly participate in and is not required for release of CO2 from glycine in the formation of the pyridoxal 5'-phosphate-quinonoid intermediate, an important distinction that is contrary to earlier findings
-
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1.4.4.2 glycine dehydrogenase (aminomethyl-transferring)
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