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Article

First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.

The Journal of biological chemistry - 23 Jan 2015

Sanyal Nikhilesh, Arentson Benjamin W, Luo Min, Tanner John J, Becker Donald F

Abstract excerpt

Proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH) catalyze the four-electron oxidation of proline to glutamate via the intermediates P5C and l-glutamate-γ-semialdehyde (GSA). In Gram-negative bacteria, PRODH and P5CDH are fused together in the bifunctional enzyme proline utilization A (PutA) whereas in other organisms PRODH and P5CDH are expressed as separate...

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Identifiers

PMID: 25492892
DOI: 10.1074/jbc.M114.625483
PMCID: PMC4303673

Genes

PRODH
SPR

Variants

Provenance

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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