Literature summary for 1.4.1.27 extracted from

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 (2010), J. Biol. Chem., 285, 18684-18692 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Escherichia coli

Crystallization (Comment)

Organism

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

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6T9	i.e. lipoyl-carrier protein component H-protein	-

Synonyms

Synonyms	Comment	Organism
GcvH	-	Escherichia coli
H-protein	-	Escherichia coli

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Release 2023.1 (January 2023)