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Article

Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase.

Proceedings of the National Academy of Sciences of the United States of America - 9 Jul 1996

Elsevier J P, Wells L, Quimby B B, Fridovich-Keil J L

Abstract excerpt

One of the fundamental questions concerning expression and function of dimeric enzymes involves the impact of naturally occurring mutations on subunit assembly and heterodimer activity. This question is of particular interest for the human enzyme galactose-l-phosphate uridylyl-transferase (GALT),...

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Identifiers

PMID: 8692963
DOI: 10.1073/pnas.93.14.7166
PMCID: PMC38954

Genes

GALT

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8692963-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

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Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase.PMID 8692963Read ↗

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A yeast expression system for human galactose-1-phosphate uridylyltransferase.Semantic proximity Read ↗

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