Literature summary for 4.3.1.7 extracted from

Shibata, N.; Higuchi, Y.; Toraya, T.
How coenzyme B12-dependent ethanolamine ammonia-lyase deals with both enantiomers of 2-amino-1-propanol as substrates: structure-based rationalization (2011), Biochemistry, 50, 591-598.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
N-terminal His6-tagged beta subunit lacking residues Lysbeta4-Cysbeta43, complexed with CN-cobalamin and (R)-2-amino-1-propanol or (S)-2-amino-1-propanol. The lower affinity for the (R)-enantiomer may be due to the conformational change of the ValR326 side chain of the enzyme. The pro-S hydrogen atom on C1 is abstracted by the adenosyl radical from both enantiomeric substrates. The NH2 group migrates from C2 to C1 by a suprafacial shift, with inversion of configuration at C1 for both enantiomeric substrates. (R)-2-amino-1-propanol is deaminated by the enzyme with inversion of configuration at C2, whereas the (S)-enantiomer is deaminated with retention. The rotameric radical intermediate from the (S)-enantiomer undergoes flipping to the rotamer from the (R)-enantiomer before the hydrogen back-abstraction, suggesting the preference of the enzyme active site for the rotamer from the (R)-enantiomer in equilibration, partly explained by steric repulsion of the (S)-enantiomer-derived product radical at C3 with the PheR329 and LeuR402 residues	Escherichia coli

Crystallization (Comment)

Organism

N-terminal His6-tagged beta subunit lacking residues Lysbeta4-Cysbeta43, complexed with CN-cobalamin and (R)-2-amino-1-propanol or (S)-2-amino-1-propanol. The lower affinity for the (R)-enantiomer may be due to the conformational change of the ValR326 side chain of the enzyme. The pro-S hydrogen atom on C1 is abstracted by the adenosyl radical from both enantiomeric substrates. The NH2 group migrates from C2 to C1 by a suprafacial shift, with inversion of configuration at C1 for both enantiomeric substrates. (R)-2-amino-1-propanol is deaminated by the enzyme with inversion of configuration at C2, whereas the (S)-enantiomer is deaminated with retention. The rotameric radical intermediate from the (S)-enantiomer undergoes flipping to the rotamer from the (R)-enantiomer before the hydrogen back-abstraction, suggesting the preference of the enzyme active site for the rotamer from the (R)-enantiomer in equilibration, partly explained by steric repulsion of the (S)-enantiomer-derived product radical at C3 with the PheR329 and LeuR402 residues

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P19636	-	-

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Release 2023.1 (January 2023)