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Article

A remote surface loop modulates core structure and cold activity in phosphopantetheine adenylyltransferase.

PloS one - 1 Jan 2026

Nam Yewon, Hwang Jisub, Kim Bogeun, Lee Jun Hyuck, Do Hackwon

Abstract excerpt

Phosphopantetheine adenylyltransferase (PPAT), a key enzyme in the universal Coenzyme A biosynthetic pathway, is essential for cellular metabolism. However, the adaptive mechanisms of PPAT in psychrophilic (cold-adapted) organisms remain poorly understood. Here, we characterize PPAT from the psychrophilic methanotroph Methylocapsa palsarum (MpaPPAT). Sequence analysis identified a unique five-amino-acid insertion...

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Share to Amino Acid Sequence
Share to Cold Temperature
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 41818184
DOI: 10.1371/journal.pone.0342296
PMCID: PMC12981448

Genes

PPAT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

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