Reaction participants Show >> << Hide
- Name help_outline (6S)-5,6,7,8-tetrahydrofolate Identifier CHEBI:57453 (Beilstein: 10223255) help_outline Charge -2 Formula C19H21N7O6 InChIKeyhelp_outline MSTNYGQPCMXVAQ-RYUDHWBXSA-L SMILEShelp_outline Nc1nc2NC[C@H](CNc3ccc(cc3)C(=O)N[C@@H](CCC([O-])=O)C([O-])=O)Nc2c(=O)[nH]1 2D coordinates Mol file for the small molecule Search links Involved in 40 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-[(R)-S8-aminomethyldihydrolipoyl]-L-lysyl-[protein]
Identifier
RHEA-COMP:10492
Reactive part
help_outline
- Name help_outline N6-[(R)-S8-aminomethyldihydrolipoyl]-L-lysine residue Identifier CHEBI:83143 Charge 1 Formula C15H30N3O2S2 SMILEShelp_outline [NH3+]CSCC[C@H](S)CCCCC(=O)NCCCC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate Identifier CHEBI:15636 (Beilstein: 5468618) help_outline Charge -2 Formula C20H21N7O6 InChIKeyhelp_outline QYNUQALWYRSVHF-OLZOCXBDSA-L SMILEShelp_outline [H][C@]12CNc3nc(N)[nH]c(=O)c3N1CN(C2)c1ccc(cc1)C(=O)N[C@@H](CCC([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
N6-[(R)-dihydrolipoyl]-L-lysyl-[protein]
Identifier
RHEA-COMP:10475
Reactive part
help_outline
- Name help_outline N6-[(R)-dihydrolipoyl]-L-lysine residue Identifier CHEBI:83100 Charge 0 Formula C14H26N2O2S2 SMILEShelp_outline SCC[C@H](S)CCCCC(=O)NCCCC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NH4+ Identifier CHEBI:28938 (CAS: 14798-03-9) help_outline Charge 1 Formula H4N InChIKeyhelp_outline QGZKDVFQNNGYKY-UHFFFAOYSA-O SMILEShelp_outline [H][N+]([H])([H])[H] 2D coordinates Mol file for the small molecule Search links Involved in 528 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:16945 | RHEA:16946 | RHEA:16947 | RHEA:16948 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system.
Okamura-Ikeda K., Fujiwara K., Motokawa Y.
T-protein, a component of the glycine cleavage system, has been purified to apparent homogeneity from chicken liver mitochondria. The molecular weight was 37,000 by sedimentation equilibrium centrifugation and 38,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave ... >> More
T-protein, a component of the glycine cleavage system, has been purified to apparent homogeneity from chicken liver mitochondria. The molecular weight was 37,000 by sedimentation equilibrium centrifugation and 38,000 by gel filtration. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave a molecular weight of 41,000, indicating that the protein is composed of a single polypeptide. A partial specific volume of 0.73 ml/g was obtained from the amino acid composition. The absorbance coefficient, A1%280nm, is 6.63 in 50 mM potassium phosphate buffer, pH 7.0. T-protein is a basic protein having a pI value of 9.8 and relatively rich in arginine rather than lysine. The protein catalyzed the degradation of the protein-bound intermediate (-CH2NH2 moiety of glycine) to a 1-carbon unit and NH3. The reaction is dependent on tetrahydrofolate (H4-folate). Apparent Km values for the intermediate and H4-folate were 3.7 microM and 0.17 mM, respectively. T-protein associated with H-protein forming a complex which was composed of one molecule each of T-protein and H-protein. Formation of the complex was not affected by the modification of the cysteinyl residues on H-protein with N-ethylmaleimide. << Less
J Biol Chem 257:135-139(1982) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.