Information on EC 2.1.2.10 - aminomethyltransferase
New: Word Map on EC 2.1.2.10
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
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[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
formation of a folate-binding cavity via the interaction of enzyme with H-protein
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[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
tetrahydrofolate is bound near the center of the tripartite enzyme, lipoic acid is bound adjacent to the tetrahydrofolate binding pocket
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[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
5-methyltetrahydrofolate is bound in a kinked shape with the pteridine group deeply buried into the hydrophobic pocket ant the glutamyl group pointed to the C-terminal side surface. R292 interacts through water molecules with the folate polyglutamate tail
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
T-protein recognition of lipoyl protein substrate and reaction mechanism, overview. The reversible transfer of the methylene group between the lipoate and tetrahydrofolate proceeds through the electron relay-assisted iminium intermediate formation
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C-N bond cleavage
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methyl group transfer
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Glycine, serine and threonine metabolism
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One carbon pool by folate
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[protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming)
A component, with EC 1.4.4.2 glycine dehydrogenase (decarboxylating) and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, formerly known as glycine synthase. The glycine cleavage system 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), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [3].
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synthase, glycine
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T-protein component of glycine cleavage complex
tetrahydrofolate aminomethyltransferase
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aminomethyltransferase
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aminomethyltransferase
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aminomethyltransferase
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GCVT
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two isogenes: GCVT-1 and GCVT-2
GCVT
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two isogenes: GCVT-1 and GCVT-2
T-protein
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T-protein component of glycine cleavage complex
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T-protein component of glycine cleavage complex
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male Wistar rats
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recombinant enzyme, expressed in Escherichia coli BL21 (DE3)pLysS
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Uniprot
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strain OT3
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strain OT3, expression in Escherichia coli
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strain OT3
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strain OT3, expression in Escherichia coli
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metabolism
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aminomethyltransferase is a component of the T-protein, which is part of a multienzyme system composed of four proteins termed P-, H-, T-, and L-protein. T-protein/aminomethyltransferase degrades the aminomethyl moiety to ammonia and 5,10-methylentetrahydrofolate in the presence of tetrahydrofolate, leaving dihydrolipoate-bearing H-protein
additional information
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T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, a complex mimicking the ternary complex in the reverse reaction, shows a highly interacting intermolecular interface limited to a small area and the protein-bound dihydrolipoyllysine arm inserted into the active site cavity of the T-protein. Arg292 of the T-protein is essential for complex assembly
physiological function
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part of glycine cleavage system, serine metabolism
physiological function
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part of glycine cleavage system, serine metabolism
physiological function
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part of glycine cleavage system, serine metabolism
physiological function
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aminomethyltransferase reversibly catalyzes the degradation of the aminomethyl moiety of glycine attached to the lipoate cofactor of H-protein, resulting in the production of ammonia, 5,10-methylenetetrahydrofolate, and dihydrolipoate-bearing H-protein in the presence of tetrahydrofolate
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reduced H-protein + 5,10-methylene-tetrahydrofolate + NH4Cl
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reduced H-protein + 5,10-methylenetetrahydropteroyltetraglutamate + NH4Cl
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
S-aminomethyldihydrolipoylprotein + tetrahydropteroyltetraglutamate
dihydrolipoylprotein + 5,10-methylenetetrahydropteroyltetraglutamate + NH3
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better substrate than 5,10-methylenetetrahydrofolate, 6.5fold higher affinity for 5,10-methylenetetrahydropteroyltetraglutamate than for 5,10-methylenetetrahydrofolate
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[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate
[protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
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r
additional information
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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aminomethyl intermediate bound to the lipoate cofactor of H-protein
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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T-protein catalyzes the tetrahydrofolate-dependent step of the glycine cleavage reaction
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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tetrahydrofolate-dependent enzyme
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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folate-binding site: Lys-78, Lys-81 and Lys-352 are involved in binding, Lys-352 may serve as the primary binding site to alpha-carboxyl group of the first glutamate residue nearest the p-aminobenzoic acid ring of 5,10-methylenetetrahydrofolate and 5,10-methylenetetrahydropteroyltetraglutamate, Lys-81 may play a key role to hold the second glutamate residue through binding to its alpha-carboxyl group, 6.5fold higher affinity for 5,10-methylenetetrahydropteroyltetraglutamate than for 5,10-methylenetetrahydrofolate
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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decarboxylated glycine moiety attached to H-protein + tetrahydrofolate as substrates
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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strictly dependent on tetrahydrofolate
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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part of the glycine cleavage system
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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requires tetrahydrofolate
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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part of the glycine cleavage system
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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important enzyme in glycine metabolism
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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T-protein catalyzes the tetrahydrofolate-dependent step of the glycine cleavage reaction
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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tetrahydrofolate-dependent enzyme
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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part of the glycine cleavage system
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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decarboxylated glycine moiety attached to H-protein + tetrahydrofolate as substrates
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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T-protein participates in the formation of the one carbon unit and ammonia or the reverse reaction
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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glycine metabolism
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additional information
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enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
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additional information
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component of the glycine cleavage system, T-protein is associated with H-protein forming a complex which is composed of one molecule of each of them
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additional information
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enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
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additional information
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enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
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additional information
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enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
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additional information
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enzyme is a component of the glycine cleavage system which is composed of P-, H-, L- and T-protein, multienzyme complex
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additional information
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enzyme is a component of the reversible glycine cleavage system which is composed of 4 protein components named as P-, H-, L- and T-protein
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate
[protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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part of the glycine cleavage system
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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part of the glycine cleavage system
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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important enzyme in glycine metabolism
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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part of the glycine cleavage system
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S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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glycine metabolism
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pyridoxal 5'-phosphate
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tetrahydrofolate
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tetrahydrofolate-dependent enzyme
tetrahydrofolate
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strictly dependent on tetrahydrofolate
tetrahydrofolate
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requires tetrahydrofolate
tetrahydrofolate
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folate-binding site; tetrahydrofolate-dependent enzyme
additional information
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H-protein with reduced lipoate
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additional information
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H-protein with reduced lipoate
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additional information
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H-protein with reduced lipoate
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iodoacetamide
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5 mM, 70% inhibition
N-ethylmaleimide
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0.1 mM, 70% inhibition
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0.0677 - 0.151
5,10-methylenetetrahydrofolate
0.0092 - 0.0382
5,10-methylenetetrahydropteroyltetraglutamate
0.00069 - 0.0169
reduced H-protein
0.0037
S-aminomethyldihydrolipoylprotein
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0.17
tetrahydrofolate
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additional information
additional information
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values for mutant enzymes
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0.0677
5,10-methylenetetrahydrofolate
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0.0869
5,10-methylenetetrahydrofolate
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mutant T4A, His-tagged
0.0875
5,10-methylenetetrahydrofolate
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mutant L6A, His-tagged
0.0881
5,10-methylenetetrahydrofolate
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wild-type with His-tag
0.151
5,10-methylenetetrahydrofolate
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N-terminal deletion mutant, His-tagged
0.0092
5,10-methylenetetrahydropteroyltetraglutamate
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wild-type with His-tag
0.0104
5,10-methylenetetrahydropteroyltetraglutamate
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0.0108
5,10-methylenetetrahydropteroyltetraglutamate
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mutant L6A, His-tagged
0.0174
5,10-methylenetetrahydropteroyltetraglutamate
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mutant T4A, His-tagged
0.0382
5,10-methylenetetrahydropteroyltetraglutamate
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N-terminal deletion mutant, His-tagged
65.4
NH4Cl
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wild-type with His-tag
78.9
NH4Cl
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mutant L6A, His-tagged
93.5
NH4Cl
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mutant T4A, His-tagged
256
NH4Cl
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N-terminal deletion mutant, His-tagged
0.00069
reduced H-protein
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wild-type with His-tag
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0.0012
reduced H-protein
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mutant T4A, His-tagged
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0.00237
reduced H-protein
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mutant L6A, His-tagged
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0.0169
reduced H-protein
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N-terminal deletion mutant, His-tagged
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2.1 - 18.4
5,10-methylenetetrahydrofolate
8.75 - 11.6
5,10-methylenetetrahydropteroyltetraglutamate
2.9 - 19.4
reduced H-protein
additional information
additional information
Escherichia coli
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values for mutant enzymes
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2.1
5,10-methylenetetrahydrofolate
Escherichia coli
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N-terminal deletion mutant, His-tagged
7.8
5,10-methylenetetrahydrofolate
Escherichia coli
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mutant T4A, His-tagged
10.3
5,10-methylenetetrahydrofolate
Escherichia coli
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mutant L6A, His-tagged
14.4
5,10-methylenetetrahydrofolate
Escherichia coli
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18.4
5,10-methylenetetrahydrofolate
Escherichia coli
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wild-type with His-tag
8.75
5,10-methylenetetrahydropteroyltetraglutamate
Escherichia coli
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9.5
5,10-methylenetetrahydropteroyltetraglutamate
Escherichia coli
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N-terminal deletion mutant, His-tagged
10.5
5,10-methylenetetrahydropteroyltetraglutamate
Escherichia coli
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wild-type with His-tag
10.6
5,10-methylenetetrahydropteroyltetraglutamate
Escherichia coli
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mutant L6A, His-tagged
11.6
5,10-methylenetetrahydropteroyltetraglutamate
Escherichia coli
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mutant T4A, His-tagged
3.9
NH4Cl
Escherichia coli
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N-terminal deletion mutant, His-tagged
9.6
NH4Cl
Escherichia coli
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mutant T4A, His-tagged
11.6
NH4Cl
Escherichia coli
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mutant L6A, His-tagged
20.9
NH4Cl
Escherichia coli
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wild-type with His-tag
2.9
reduced H-protein
Escherichia coli
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N-terminal deletion mutant, His-tagged
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8.5
reduced H-protein
Escherichia coli
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mutant T4A, His-tagged
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13.3
reduced H-protein
Escherichia coli
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mutant L6A, His-tagged
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19.4
reduced H-protein
Escherichia coli
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wild-type with His-tag
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additional information
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additional information
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pI: 9.8
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37
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assay at
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Bacillus subtilis (strain 168)
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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37000 - 38000
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sedimentation equilibrium centrifugation, gel filtration
57000
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T-protein in complex with H-protein, gel filtration
75000
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dynamic light scattering
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dimer
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2 * 46170, calculated
dimer
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crystallization data, cloverleaf-like orientation of protomer around a central hole
dimer
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2 * 46170, calculated; crystallization data, cloverleaf-like orientation of protomer around a central hole
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monomer
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conformational change after interaction with H-protein
monomer
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1 * 41000, SDS-PAGE
monomer
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1 * 45000, lithium dodecyl sulfate PAGE
monomer
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conformational change after interaction with H-protein
additional information
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construction of low-resolution model and tertiary structure model
additional information
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interaction of enzyme with H-protein
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aminomethyltransferase/T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, a complex mimicking the ternary complex in the reverse reaction, purified recombinant wild-type and mutant T-proteins, hanging drop vapor diffusion method, mixing of 22-25 mg/ml proteins, T-protein and H protein, with an equal volume of reservoir solution containing 0.095 M 2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid, pH 7.5, 0.19 M calcium chloride, 26.6% v/v PEG 400, and 5% v/v glycerol, at 15°C, 4-5 days to 2 weeks, soaking of the native crystals in mother liquid containing 1 mM (6S)-5-methyltetrahydrofolate at 15°C for 4 h, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
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apoform and bound to 5-methyltetrahydrofolate
apoform, tetrahydrofolate complex, folinic acid complex and lipoic acid complex of enzyme, homology model of human enzyme
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50
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1 min, 20% loss of activity
70
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1 min, complete loss of activity
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lability of enzyme under the conditions of its purifications and storage
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-20°C, 20 mM Tris-HCl buffer, pH 8.0, 10 mM 2-mercaptoethanol, 50% v/v glycerol, at least 2 months, stable
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-20°C, 24 h, 60% loss of activity
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purification of recombinant enzyme, expressed in Escherichia coli BL21 (DE3)pLysS, and of mutants
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Amt gene is located on chromosome 3p21 and contains 9 exons spanning about 6 kb of genomic sequence
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C-terminally His6-tagged T-protein wild-type and mutant enzymes expression in Escherichia coli strain BL21(DE3)pLysS
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cloning and sequencing of the Amt gene with 9 closely spaced exons that are contained within about 5 kb of genomic DNA, encoding a protein of 403 amino acids, cis-acting promoter is likely to be very short, Amt gene may be localized on chromosome 9F
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transfection to Leishmania infantum and Leishmania major
transfection to Leishmania infantum and Leishmania major
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transfection to Leishmania infantum and Leishmania major
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decrease of expression of isogene 1 of T-protein component of glcycine cleavage complex in amastigote growth
increased expression upon exposure to light
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response to heat stress in higher expression of isogene 1 of T-protein component of glcycine cleavage complex, inducible expression upon excess glycine
decrease of expression of isogene 1 of T-protein component of glcycine cleavage complex in amastigote growth
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decrease of expression of isogene 1 of T-protein component of glcycine cleavage complex in amastigote growth
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response to heat stress in higher expression of isogene 1 of T-protein component of glcycine cleavage complex, inducible expression upon excess glycine
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response to heat stress in higher expression of isogene 1 of T-protein component of glcycine cleavage complex, inducible expression upon excess glycine
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D96N
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site-directed mutagenesis, both the glycine cleavage and synthesis activities are reduced to 34% compared to the wild-type enzyme
D96N/Y188F
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site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
D97N
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
D97N/Y188F
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site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
K352E
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mutant with 2fold increased Km-values for folate substrates
K352Q
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mutant with 2fold increased Km-values for folate substrates
K352R
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no effect on Km-values
K75E
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mutant with 2.5fold increased Km-value for 5,10-methylenetetrahydrofolate and 8fold increased Km-value for 5,10-methylenetetrahydropteroyltetraglutamate
K78E
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mutant with 1.4fold increased Km-values for folate substrates
K81E
-
mutant with 3fold increased Km-value for 5,10-methylenetetrahydrofolate and 16fold increased Km-value for 5,10-methylenetetrahydropteroyltetraglutamate
L6A
-
in contrast to wild-type, quite susceptible to trypsinolysis, 4fold increase in Km-value for reduced H-protein
N113A
-
site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
N113A/R223A
-
site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
N113D
-
site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
R223A
-
site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
R223K
-
site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
T4A
-
2fold increase in Km-value for reduced H-protein
Y188F
-
site-directed mutagenesis, both the glycine cleavage and synthesis activities are reduced to 83% compared to the wild-type enzyme
D276H
-
nonketotic hyperglycinemia, rare mutation
E211K
-
polymorphism occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
G269D
-
nonketotic hyperglycinemia, rare mutation
G47R
-
nonketotic hyperglycinemia, rare mutation
H42R
-
present in many nonketotic hyperglycinemia affected members of an extended Israeli-Arab kindred
N117I
-
mutant may cause nonketotic hygerglycinemia
N145I
-
nonketotic hyperglycinemia, substitution of conserved N, patient has servere neonatal presentation and died in the newborn period
Q192X
-
nonketotic hyperglycinemia, premature stop codon
R296H
-
mutation occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
R318R
-
polymorphism occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
R320H
-
allele frequency of 7% for R320H of T-protein in 50 patients with enzymatic confirmation of their diagnostics of nonketotic hyperglycinemia
additional information
-
N-terminal deletion of 7 amino acids, in contrast to wild-type, quite susceptible to trypsinolysis
additional information
-
allele frequency of 3% for T-protein splice site mutation IVS7-1G-A in 50 patients with enzymatic confirmation of their diagnostics of nonketotic hyperglycinemia, mutation with a one-base deletion 183delC
additional information
-
a subset of nonketotic hyperglycinemia cases is due to mutations in the gene for the T-protein
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medicine
-
strategy for molecular investigation of patients with nonketotic hyperglycinemia: defective glycine cleavage enzyme system, composed of P-, H-, T- and L-protein, 15% of patients have a T-protein defect
medicine
-
a subset of nonketotic hyperglycinemia cases is due to mutations in the gene for the T-protein
medicine
-
identification of several mutations and polymorphisms occurring in patients with glycine encephalopathy, NKH, and methods for their PCR-restriction enzyme analysis
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Hyperglycinemia, Nonketotic
Identification of a common mutation in Finnish patients with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Identification of the first reported splice site mutation (IVS7-1G-->A) in the aminomethyltransferase (T-protein) gene (AMT) of the glycine cleavage complex in 3 unrelated families with nonketotic hyperglycinemia.
Hyperglycinemia, Nonketotic
Mutation analysis of glycine decarboxylase, aminomethyltransferase and glycine cleavage system protein-H genes in 13 unrelated families with glycine encephalopathy.
Leukemia
Genomic organization of the dog dystroglycan gene DAG1 locus on chromosome 20q15.1-q15.2.
Leukemia, T-Cell
Genomic structures and sequences of two closely linked genes (AMT, TCTA) on dog chromosome 20q15.1-->q15.2.
Neoplasms
Proteomic analysis of the effect of retinoic acids on the human breast cancer cell line MCF-7.
Propionic Acidemia
Inhibition of glycine synthase by branched-chain alpha-keto acids. A possible mechanism for abnormal glycine metabolism in ketotic hyperglycinemia.
Vitamin B 12 Deficiency
The vitamin B12-deficient rat as a possible model of ketotic hyperglycinemia.
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Bourguignon, J.; Neuburger, M.; Douce, R.
Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase
Biochem. J.
255
169-178
1988
Pisum sativum
brenda
Motokawa, Y.; Kikuchi, G.
Glycine metabolism by rat liver mitochondria. Reconstruction of the reversible glycine cleavage system with partially purified protein components
Arch. Biochem. Biophys.
164
624-633
1974
Rattus norvegicus
brenda
Okamura-Ikeda, K.; Fujiwara, K.; Motokawa, Y.
Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system
J. Biol. Chem.
257
135-139
1982
Gallus gallus
brenda
Toone, J.R.; Applegarth, D.A.; Coulter-Mackie, M.B.; James, E.R.
Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): A strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH)
Mol. Genet. Metab.
72
322-325
2001
Homo sapiens
brenda
Backofen, B.; Leeb, T.
Genomic organization of the murine aminomethyltransferase gene (Amt)
DNA Seq.
13
179-183
2002
Homo sapiens, Mus musculus
brenda
Okamura-Ikeda, K.; Fujiwara, K.; Motokawa, Y.
Identification of the folate binding sites on the Escherichia coli T-protein of the glycine cleavage system
J. Biol. Chem.
274
17471-17477
1999
Escherichia coli
brenda
Lokanath, N.K.; Kuroishi, C.; Okazaki, N.; Kunishima, N.
Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3
Acta Crystallogr. Sect. D
60
1450-1452
2004
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Orun, O.; Koch, M.H.; Kan, B.; Svergun, D.I.; Petoukhov, M.V.; Sayers, Z.
Structural characterization of T-protein of the Escherichia coli glycine cleavage system by X-ray small angle scattering
Cell. Mol. Biol.
49
453-459
2003
Escherichia coli
-
brenda
Okamura-Ikeda, K.; Kameoka, N.; Fujiwara, K.; Motokawa, Y.
Probing the H-protein-induced conformational change and the function of the N-terminal region of Escherichia coli T-protein of the glycine cleavage system by limited proteolysis
J. Biol. Chem.
278
10067-10072
2003
Escherichia coli
brenda
Lee, H.H.; Kim do, J.; Ahn, H.J.; Ha, J.Y.; Suh, S.W.
Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia
J. Biol. Chem.
279
50514-50523
2004
Thermotoga maritima
brenda
Okamura-Ikeda, K.; Hosaka, H.; Yoshimura, M.; Yamashita, E.; Toma, S.; Nakagawa, A.; Fujiwara, K.; Motokawa, Y.; Taniguchi, H.
Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia
J. Mol. Biol.
351
1146-1159
2005
Homo sapiens (P48728)
brenda
Toone, J.R.; Applegarth, D.A.; Levy, H.L.; Coulter-Mackie, M.B.; Lee, G.
Molecular genetic and potential biochemical characteristics of patients with T-protein deficiency as a cause of glycine encephalopathy (NKH)
Mol. Genet. Metab.
79
272-280
2003
Homo sapiens
brenda
Lokanath, N.K.; Kuroishi, C.; Okazaki, N.; Kunishima, N.
Crystal structure of a component of glycine cleavage system: T-protein from Pyrococcus horikoshii OT3 at 1.5 A resolution
Proteins
58
769-773
2005
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
brenda
Mueller, M.; Papadopoulou, B.
Stage-specific expression of the glycine cleavage complex subunits in Leishmania infantum
Mol. Biochem. Parasitol.
170
17-27
2010
Leishmania infantum, Leishmania major
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
Escherichia coli, Homo sapiens, Pisum sativum
brenda
Okamura-Ikeda, K.; Hosaka, H.; Maita, N.; Fujiwara, K.; Yoshizawa, A.C.; Nakagawa, A.; Taniguchi, H.
Crystal structure of aminomethyltransferase in complex with dihydrolipoyl-H-protein of the glycine cleavage system: implications for recognition of lipoyl protein substrate, disease-related mutations, and reaction mechanism
J. Biol. Chem.
285
18684-18692
2010
Escherichia coli
brenda
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Enzyme Nomenclature
COMMENTARY
2.1.2.10-RECOMMENDED NAME
[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
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