Literature summary for 1.4.4.2 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.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
glycine + H-protein-lipoyllysine	Escherichia coli	-	H-protein-S-aminomethyldihydrolipoyllysine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
glycine + H-protein-lipoyllysine	-	Escherichia coli	H-protein-S-aminomethyldihydrolipoyllysine + CO2	-	?

Synonyms

Synonyms	Comment	Organism
P-protein	part of the glycine cleavage system	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Escherichia coli

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Release 2023.1 (January 2023)