ArticleMolecular and cellular biochemistry2002
Human liver AMP-deaminase--oligomeric forms of the enzyme.
Article in Molecular and cellular biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Deciphering AMP deaminase-2 structure, activators and regulators underpinning cellular function in human fructose and nucleotide metabolism.bioRxiv : the preprint server for biology · 2026Article
- Expression patterns of AMP-deaminase isozymes in human hepatocellular carcinoma (HCC).Molecular and cellular biochemistry · 2008Article
- Expression patterns of AMP-deaminase and cytosolic 5'-nucleotidase genes in human term placenta.Molecular and cellular biochemistry · 2008Article
- Full-size form of human liver AMP-deaminase?Molecular and cellular biochemistry · 2004Article
- AMP-deaminase from normal and cirrhotic human liver: a comparative study.Molecular and cellular biochemistry · 2004Article
- AMP-deaminase from human term placenta.Molecular and cellular biochemistry · 2003Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AMP-deaminase (EC 3.5.4.6) is a key enzyme of nucleotide breakdown involved in regulation of adenine nucleotide pool in the liver. Mechanisms regulating activity of the enzyme are not completely elucidated, till now. In this paper experimental data indicating on the potential regulatory significance of changes in oligomeric structure of the enzyme are presented. SDS-PAG electrophoresis of human liver AMP-deaminase revealed the presence of three enzyme fragments. Only largest of them (the protein fragments weighing 68 kDa) reacted immunologically with anti- (human liver) AMP-deaminase antibodies. At physiological pH 7.0, in the absence of regulatory ligands, reaction catalysed by human liver AMP-deaminase was strongly dependent on enzyme concentration used, with half-saturation constant (S0.5) values increasing significantly with the degree of enzyme dilution. Preincubation with activated long-chain fatty acids--substances promoting dissociation of oligomeric enzymes, inhibited the activity of AMP-deaminase studied nearly completely. Gel filtration on Sepharose CL-6B column demonstrated existence of at least three active oligomeric forms of human liver AMP-deaminase. We postulate that oligomeric structure of the enzyme is a factor determining regulatory profile of AMP-deaminase studied.
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