Literature summary for 4.3.1.7 extracted from

Shibata, N.; Tamagaki, H.; Hieda, N.; Akita, K.; Komori, H.; Shomura, Y.; Terawaki, S.; Mori, K.; Yasuoka, N.; Higuchi, Y.; Toraya, T.
Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates (2010), J. Biol. Chem., 285, 26484-26493.

Cloned(Commentary)

Cloned (Comment)	Organism
N-terminal His6-tagged beta subunit lacking residues Lysbeta4-Cysbeta43	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
N-terminal His6-tagged beta subunit lacking residues Lysbeta4-Cysbeta43, in complex with cyanocobalamin and in complex with cyanocobalamin or adeninylpentylcobalamin and substrates. The enzyme exists as a trimer of the (alphabeta)2 dimer. The active site is in the (beta/alpha)8 barrel of the-subunit, the beta-subunit covers the lower part of the cobalamin that is bound in the interface of the alpha- and beta-subunits. The structure complexed with adeninylpentylcobalamin reveals the presence of an adenine ring-binding pocket in the enzyme that accommodates the adenine moiety through a hydrogen bond network. The substrate is bound by six hydrogen bonds with active-site residues. Arg160 contributes to substrate binding most likely by hydrogen bonding with the O1 atom. Marked angular strains and tensile forces induced by tight enzyme-coenzyme interactions are responsible for breaking the coenzyme-Co-C bond. A major structural change upon substrate binding is not observed with this particular enzyme. Glu287, one of the substrate-binding residues, has a direct contact with the ribose group of the modeled adenosylcobalamin, which may contribute to the substrate-induced additional labilization of the Co-C bond	Escherichia coli

Crystallization (Comment)

Organism

N-terminal His6-tagged beta subunit lacking residues Lysbeta4-Cysbeta43, in complex with cyanocobalamin and in complex with cyanocobalamin or adeninylpentylcobalamin and substrates. The enzyme exists as a trimer of the (alphabeta)2 dimer. The active site is in the (beta/alpha)8 barrel of the-subunit, the beta-subunit covers the lower part of the cobalamin that is bound in the interface of the alpha- and beta-subunits. The structure complexed with adeninylpentylcobalamin reveals the presence of an adenine ring-binding pocket in the enzyme that accommodates the adenine moiety through a hydrogen bond network. The substrate is bound by six hydrogen bonds with active-site residues. Arg160 contributes to substrate binding most likely by hydrogen bonding with the O1 atom. Marked angular strains and tensile forces induced by tight enzyme-coenzyme interactions are responsible for breaking the coenzyme-Co-C bond. A major structural change upon substrate binding is not observed with this particular enzyme. Glu287, one of the substrate-binding residues, has a direct contact with the ribose group of the modeled adenosylcobalamin, which may contribute to the substrate-induced additional labilization of the Co-C bond

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P19636	-	-

Cofactor

Cofactor	Comment	Organism	Structure
adenosylcobalamin	marked angular strains and tensile forces induced by tight enzyme-coenzyme interactions are responsible for breaking the coenzyme-Co-C bond. A major structural change upon substrate binding is not observed with this particular enzyme. Glu287, one of the substrate-binding residues, has a direct contact with the ribose group of the modeled adenosylcobalamin, which may contribute to the substrate-induced additional labilization of the Co-C bond	Escherichia coli