Literature summary for 4.1.1.11 extracted from

Lee, B.I.; Suh, S.W.
Crystal structure of the Schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase (2004), J. Mol. Biol., 340, 1-7.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
both apo form and in complex with isoasparagine	Helicobacter pylori

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pylori	P56065	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	self-processing of subunits at Gly24-Ser25 producing beta-chain with residues 1-24 and alpha chain with residues 25-117. In the apo structure, Ser25, which forms the N-terminus of alpha chain, is converted to a pyruvoyl group	Helicobacter pylori

Reaction

Reaction	Comment	Organism	Reaction ID
L-aspartate = beta-alanine + CO2	in the apo structure, N-terminal Ser25 of alpha chain is converted to pyruvoyl group. Substrate analogue isoasparagine becomes covalently attached to the pyruvoyl group forming the Schiff base intermediate prior to decarboxylation	Helicobacter pylori	a

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Release 2023.1 (January 2023)