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Article

AMP inhibition of pig kidney fructose-1,6-bisphosphatase.

Biochimica et biophysica acta - 9 Jul 2001

Kelley-Loughnane N, Kantrowitz E R

Abstract excerpt

Lys-112 and Tyr-113 in pig kidney fructose-1,6-bisphosphatase (FBPase) make direct interactions with AMP in the allosteric binding site. Both residues interact with the phosphate moiety of AMP while Tyr-113 also interacts with the 3'-hydroxyl of the ribose ring. The role of these two residues in AMP binding and allosteric inhibition was investigated. Site-specific mutagenesis was used to convert Lys-112 to...

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Identifiers

PMID: 11451439
DOI: 10.1016/s0167-4838(01)00218-7

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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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