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1.4.1.27: glycine cleavage system

This is an abbreviated version!
For detailed information about glycine cleavage system, go to the full flat file.

Word Map on EC 1.4.1.27

Reaction

glycine
+
tetrahydrofolate
 +
NAD+
=
5,10-methylenetetrahydrofolate
 +
NH3
 +
CO2
 +
NADH

Synonyms

Amt, At1g11860, At1g32470, At1g48030, AT2G35370, At4g33010, DLD, DLDH, GCSH, GCV, GcvH, GcvP, GCVT, GDCSH, GDCSP, GDH1, GDSCT, GLDC, glycine cleavage complex, H-protein, LpdA, P-protein, sll0171, slr1096, T-protein

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.1 With NAD+ or NADP+ as acceptor
                1.4.1.27 glycine cleavage system

Crystallization

Crystallization on EC 1.4.1.27 - glycine cleavage system

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
component T-protein in complex with dihydrolipoate-bearing H-protein and 5-methyltetrahydrofolate, mimicking the ternary complex in the reverse reaction. The complex 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. Invariant residue Arg292 of the T-protein is essential for complex assembly
structure of component T-protein, at 1.5 A resolution. The dimeric state might be essential for the function. The role of residue Glu100 might be the activation of the N10 atom of tetrahodrofolate by increasing its nucleophilic character. The H-protein-T-protein interface includes invariant residues Arg327, Tyr330, and Arg376 of domain III, and Lys20, Phe24, Gly26, Ser35, Ile36, Leu248, Gly249, Asp252, Thr253, Arg255, and Leu262 of domains I and II
structures of component T-protein in the apoform, the tetrahydrofolate complex, the folinic acid complex, and the lipoic acid complex. Tetrahydrofolate (or folinic acid) is bound near the center of the tripartite T-protein. Lipoic acid is bound adjacent to the tetrahydrofolate binding pocket, thus defining the interaction surface for H-protein binding