The role of adenosine monophosphate nucleosidase in the regulation of adenine nucleotide levels in Azotobacter vinelandii during aerobic-anaerobic transitions

Hazel B. Leung, Vern L. Schramm

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8 Citations (Scopus)

Abstract

When cultures of Azotobacter vinelandii are made anaerobic the adenylate pool size remains constant or increases slightly while the adenylate energy charge decreases. Under these conditions, cell growth stops but the cells remain viable for at least 5 h with the decreased energy charge. The changes in the adenylate pool during the aerobic-anaerobic transition include: the formation of adenylates as a result of RNA degradation; the degradation of a portion of the excess AMP to form hypoxanthine by the sequential actions of AMP nucleosidase and adenine deaminase; an increase in the total adenylate pool which is stabilized at approximately 1.5 times the level in growing cells; and stabilization of the adenylate energy charge at a value near 0.3. The degradation of AMP is regulated by AMP nucleosidase, an allosteric enzyme which is activated by MgATP2- and inhibited by Pi. The in vivo activity of AMP nucleosidase was estimated by measuring the rate of hypoxanthine formation in the culture or by measuring the activity of purified enzyme at the concentrations of AMP, ATP, and Pi found in the cells. The maximum estimated in vivo rate of AMP degradation was less than 3% of the catalytic capacity of AMP nucleosidase. Thus ample activity is present for rapid adjustments of the AMP levels in these cells. Expression of AMP nucleosidase catalytic activity is tightly controlled since high constant concentrations of intracellular AMP can be maintained for extended time periods at low adenylate energy charge values. Under these conditions controlled degradation of AMP can occur to maintain a constant AMP concentration.

Original languageEnglish (US)
Pages (from-to)46-56
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume190
Issue number1
DOIs
StatePublished - 1978
Externally publishedYes

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adenosine nucleosidase
N-Glycosyl Hydrolases
Azotobacter vinelandii
AMP nucleosidase
Adenine Nucleotides
Adenosine Monophosphate
Degradation
Hypoxanthine
adenine deaminase
AMP Deaminase
RNA Stability
Cell growth
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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title = "The role of adenosine monophosphate nucleosidase in the regulation of adenine nucleotide levels in Azotobacter vinelandii during aerobic-anaerobic transitions",
abstract = "When cultures of Azotobacter vinelandii are made anaerobic the adenylate pool size remains constant or increases slightly while the adenylate energy charge decreases. Under these conditions, cell growth stops but the cells remain viable for at least 5 h with the decreased energy charge. The changes in the adenylate pool during the aerobic-anaerobic transition include: the formation of adenylates as a result of RNA degradation; the degradation of a portion of the excess AMP to form hypoxanthine by the sequential actions of AMP nucleosidase and adenine deaminase; an increase in the total adenylate pool which is stabilized at approximately 1.5 times the level in growing cells; and stabilization of the adenylate energy charge at a value near 0.3. The degradation of AMP is regulated by AMP nucleosidase, an allosteric enzyme which is activated by MgATP2- and inhibited by Pi. The in vivo activity of AMP nucleosidase was estimated by measuring the rate of hypoxanthine formation in the culture or by measuring the activity of purified enzyme at the concentrations of AMP, ATP, and Pi found in the cells. The maximum estimated in vivo rate of AMP degradation was less than 3{\%} of the catalytic capacity of AMP nucleosidase. Thus ample activity is present for rapid adjustments of the AMP levels in these cells. Expression of AMP nucleosidase catalytic activity is tightly controlled since high constant concentrations of intracellular AMP can be maintained for extended time periods at low adenylate energy charge values. Under these conditions controlled degradation of AMP can occur to maintain a constant AMP concentration.",
author = "Leung, {Hazel B.} and Schramm, {Vern L.}",
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T1 - The role of adenosine monophosphate nucleosidase in the regulation of adenine nucleotide levels in Azotobacter vinelandii during aerobic-anaerobic transitions

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N2 - When cultures of Azotobacter vinelandii are made anaerobic the adenylate pool size remains constant or increases slightly while the adenylate energy charge decreases. Under these conditions, cell growth stops but the cells remain viable for at least 5 h with the decreased energy charge. The changes in the adenylate pool during the aerobic-anaerobic transition include: the formation of adenylates as a result of RNA degradation; the degradation of a portion of the excess AMP to form hypoxanthine by the sequential actions of AMP nucleosidase and adenine deaminase; an increase in the total adenylate pool which is stabilized at approximately 1.5 times the level in growing cells; and stabilization of the adenylate energy charge at a value near 0.3. The degradation of AMP is regulated by AMP nucleosidase, an allosteric enzyme which is activated by MgATP2- and inhibited by Pi. The in vivo activity of AMP nucleosidase was estimated by measuring the rate of hypoxanthine formation in the culture or by measuring the activity of purified enzyme at the concentrations of AMP, ATP, and Pi found in the cells. The maximum estimated in vivo rate of AMP degradation was less than 3% of the catalytic capacity of AMP nucleosidase. Thus ample activity is present for rapid adjustments of the AMP levels in these cells. Expression of AMP nucleosidase catalytic activity is tightly controlled since high constant concentrations of intracellular AMP can be maintained for extended time periods at low adenylate energy charge values. Under these conditions controlled degradation of AMP can occur to maintain a constant AMP concentration.

AB - When cultures of Azotobacter vinelandii are made anaerobic the adenylate pool size remains constant or increases slightly while the adenylate energy charge decreases. Under these conditions, cell growth stops but the cells remain viable for at least 5 h with the decreased energy charge. The changes in the adenylate pool during the aerobic-anaerobic transition include: the formation of adenylates as a result of RNA degradation; the degradation of a portion of the excess AMP to form hypoxanthine by the sequential actions of AMP nucleosidase and adenine deaminase; an increase in the total adenylate pool which is stabilized at approximately 1.5 times the level in growing cells; and stabilization of the adenylate energy charge at a value near 0.3. The degradation of AMP is regulated by AMP nucleosidase, an allosteric enzyme which is activated by MgATP2- and inhibited by Pi. The in vivo activity of AMP nucleosidase was estimated by measuring the rate of hypoxanthine formation in the culture or by measuring the activity of purified enzyme at the concentrations of AMP, ATP, and Pi found in the cells. The maximum estimated in vivo rate of AMP degradation was less than 3% of the catalytic capacity of AMP nucleosidase. Thus ample activity is present for rapid adjustments of the AMP levels in these cells. Expression of AMP nucleosidase catalytic activity is tightly controlled since high constant concentrations of intracellular AMP can be maintained for extended time periods at low adenylate energy charge values. Under these conditions controlled degradation of AMP can occur to maintain a constant AMP concentration.

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