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Article

Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer.

Nature communications - 31 Jul 2017

Maderbocus Riyaz, Fields Blanche L, Hamilton Keith, Luo Shukun, Tran Timothy H, Dietrich Lars E P, Tong Liang

Abstract excerpt

Pseudomonas species and other aerobic bacteria have a biotin-independent malonate decarboxylase that is crucial for their utilization of malonate as the sole carbon and energy source. The malonate decarboxylase holoenzyme contains four subunits, having an acyl-carrier protein (MdcC subunit) with a distinct prosthetic group, as well as decarboxylase (MdcD-MdcE) and acyl-carrier protein transferase (MdcA) catalytic...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 28757619
DOI: 10.1038/s41467-017-00233-z
PMCID: PMC5534430

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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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