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Article

Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase.

Structure (London, England : 1993) - 15 Apr 2009

Chen Hui-Ju, Ko Tzu-Ping, Lee Chia-Yin, Wang Nai-Chen, Wang Andrew H-J

Abstract excerpt

The type-I PLP enzyme l-aspartate beta-decarboxylase converts aspartate to alanine and CO(2). Similar to the homodimeric aminotransferases, its protein subunit comprises a large and a small domain, of 410 and 120 residues, respectively. The crystal structure reveals a dodecamer made of six identical dimers arranged in a truncated tetrahedron whose assembly involves tetramer and hexamer as intermediates. The...

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Identifiers

PMID: 19368885
DOI: 10.1016/j.str.2009.02.013

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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