Literature summary for 4.3.1.7 extracted from

Shibata, N.; Tamagaki, H.; Ohtsuki, S.; Hieda, N.; Akita, K.; Komori, H.; Shomura, Y.; Terawaki, S.; Toraya, T.; Yasuoka, N.; Higuchi, Y.
Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli (2010), Acta Crystallogr. Sect. F, 66, 709-711.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
deletion mutants of the enzyme beta subunit DELTA4-30 and DELTA4-43, to 8.0 and 2.1 A resolution, respcetively	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	Overexpression of deletion mutants of the enzyme beta subunit DELTA4-30 and DELTA4-43. N-terminal truncation of the Escherichia coli EAL beta-subunit dramatically increases the solubility of the enzyme without altering its catalytic properties	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P19636	-	-

Purification (Commentary)

Purification (Comment)	Organism
N-terminal truncation of the Escherichia coli EAL beta-subunit dramatically increases the solubility of the enzyme without altering its catalytic properties	Escherichia coli

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Release 2023.1 (January 2023)