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[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
P48728
[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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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
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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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r
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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r
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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r
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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r
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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r
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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requires tetrahydrofolate
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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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r
S-aminomethyldihydrolipoylprotein + (6S)-tetrahydrofolate
dihydrolipoylprotein + (6R)-5,10-methylenetetrahydrofolate + NH3
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strictly dependent on tetrahydrofolate
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r
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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r
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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part of the glycine cleavage system
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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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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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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
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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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part of the glycine cleavage system
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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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[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate
[protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
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r
0.0677
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5,10-methylenetetrahydrofolate
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0.0869
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5,10-methylenetetrahydrofolate
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mutant T4A, His-tagged
0.0875
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5,10-methylenetetrahydrofolate
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mutant L6A, His-tagged
0.0881
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5,10-methylenetetrahydrofolate
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wild-type with His-tag
0.151
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5,10-methylenetetrahydrofolate
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N-terminal deletion mutant, His-tagged
0.0092
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5,10-methylenetetrahydropteroyltetraglutamate
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wild-type with His-tag
0.0104
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5,10-methylenetetrahydropteroyltetraglutamate
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0.0108
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5,10-methylenetetrahydropteroyltetraglutamate
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mutant L6A, His-tagged
0.0174
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5,10-methylenetetrahydropteroyltetraglutamate
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mutant T4A, His-tagged
65.4
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NH4Cl
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wild-type with His-tag
78.9
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NH4Cl
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mutant L6A, His-tagged
93.5
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NH4Cl
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mutant T4A, His-tagged
256
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NH4Cl
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N-terminal deletion mutant, His-tagged
0.00069
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reduced H-protein
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wild-type with His-tag
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0.0012
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reduced H-protein
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mutant T4A, His-tagged
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0.00237
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reduced H-protein
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mutant L6A, His-tagged
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0.0169
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reduced H-protein
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N-terminal deletion mutant, His-tagged
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0.0037
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S-Aminomethyldihydrolipoylprotein
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0.17
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tetrahydrofolate
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0.0382
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5,10-methylenetetrahydropteroyltetraglutamate
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N-terminal deletion mutant, His-tagged
additional information
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additional information
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values for mutant enzymes
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2.1
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5,10-methylenetetrahydrofolate
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N-terminal deletion mutant, His-tagged
7.8
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5,10-methylenetetrahydrofolate
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mutant T4A, His-tagged
10.3
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5,10-methylenetetrahydrofolate
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mutant L6A, His-tagged
14.4
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5,10-methylenetetrahydrofolate
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18.4
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5,10-methylenetetrahydrofolate
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wild-type with His-tag
8.75
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5,10-methylenetetrahydropteroyltetraglutamate
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9.5
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5,10-methylenetetrahydropteroyltetraglutamate
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N-terminal deletion mutant, His-tagged
10.5
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5,10-methylenetetrahydropteroyltetraglutamate
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wild-type with His-tag
10.6
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5,10-methylenetetrahydropteroyltetraglutamate
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mutant L6A, His-tagged
3.9
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NH4Cl
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N-terminal deletion mutant, His-tagged
9.6
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NH4Cl
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mutant T4A, His-tagged
11.6
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NH4Cl
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mutant L6A, His-tagged
20.9
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NH4Cl
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wild-type with His-tag
2.9
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reduced H-protein
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N-terminal deletion mutant, His-tagged
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8.5
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reduced H-protein
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mutant T4A, His-tagged
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13.3
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reduced H-protein
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mutant L6A, His-tagged
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19.4
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reduced H-protein
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wild-type with His-tag
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11.6
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5,10-methylenetetrahydropteroyltetraglutamate
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mutant T4A, His-tagged
additional information
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additional information
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values for mutant enzymes
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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
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mutant with 3fold increased Km-value for 5,10-methylenetetrahydrofolate and 16fold increased Km-value for 5,10-methylenetetrahydropteroyltetraglutamate
N113A
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
N113A/R223A
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site-directed mutagenesis, the mutations abolish both the glycine cleavage and synthesis activities
N113D
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
R223A
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
R223K
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site-directed mutagenesis, the mutation abolishes both the glycine cleavage and synthesis activities
T4A
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2fold increase in Km-value for reduced H-protein
Y188F
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site-directed mutagenesis, both the glycine cleavage and synthesis activities are reduced to 83% compared to the wild-type enzyme
D276H
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nonketotic hyperglycinemia, rare mutation
E211K
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polymorphism occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
G269D
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nonketotic hyperglycinemia, rare mutation
G47R
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nonketotic hyperglycinemia, rare mutation
N117I
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mutant may cause nonketotic hygerglycinemia
N145I
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nonketotic hyperglycinemia, substitution of conserved N, patient has servere neonatal presentation and died in the newborn period
Q192X
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nonketotic hyperglycinemia, premature stop codon
R296H
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mutation occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
R318R
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polymorphism occurring in patients with glycine encephalopathy, NKH, method for PCR-restriction enzyme analysis
R320H
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allele frequency of 7% for R320H of T-protein in 50 patients with enzymatic confirmation of their diagnostics of nonketotic hyperglycinemia
L6A
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in contrast to wild-type, quite susceptible to trypsinolysis, 4fold increase in Km-value for reduced H-protein
additional information
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N-terminal deletion of 7 amino acids, in contrast to wild-type, quite susceptible to trypsinolysis
H42R
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present in many nonketotic hyperglycinemia affected members of an extended Israeli-Arab kindred
additional information
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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
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a subset of nonketotic hyperglycinemia cases is due to mutations in the gene for the T-protein
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Enzyme Nomenclature
----[protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH3
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